GB1565190A - Recombinant dna transfer vector and microorganism containing a gene from a higher organism - Google Patents

Recombinant dna transfer vector and microorganism containing a gene from a higher organism Download PDF

Info

Publication number: GB1565190A
Authority: GB; United Kingdom
Prior art keywords: dna; nucleotide sequence; transfer vector; mrna; microorganism
Prior art date: 1977-05-27
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Expired

Application number

GB22417/78A

Other languages

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

University of California Berkeley

University of California San Diego UCSD

Original Assignee

University of California Berkeley

University of California San Diego UCSD

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1977-05-27

Filing date

1978-05-25

Publication date

1980-04-16

1978-04-19 Priority claimed from US05897710 external-priority patent/US4363877B1/en

1978-04-21 Priority claimed from US05/898,887 external-priority patent/US4264731A/en

1978-05-25 Application filed by University of California Berkeley, University of California San Diego UCSD filed Critical University of California Berkeley

1979-07-30 Priority to GB7926492A priority Critical patent/GB2027610B/en

1980-04-16 Publication of GB1565190A publication Critical patent/GB1565190A/en

1984-12-31 Priority to MY1984121A priority patent/MY8400121A/xx

Status Expired legal-status Critical Current

Links

108090000623 proteins and genes Proteins 0.000 title claims abstract description 123
238000012546 transfer Methods 0.000 title claims abstract description 101
239000013598 vector Substances 0.000 title claims abstract description 90
244000005700 microbiome Species 0.000 title claims abstract description 71
108020004511 Recombinant DNA Proteins 0.000 title description 8
239000002773 nucleotide Substances 0.000 claims abstract description 115
125000003729 nucleotide group Chemical group 0.000 claims abstract description 115
239000002299 complementary DNA Substances 0.000 claims abstract description 102
108020004999 messenger RNA Proteins 0.000 claims abstract description 92
102000004169 proteins and genes Human genes 0.000 claims abstract description 63
108091032973 (ribonucleotides)n+m Proteins 0.000 claims abstract description 42
239000000122 growth hormone Substances 0.000 claims abstract description 35
102000018997 Growth Hormone Human genes 0.000 claims abstract description 33
108010051696 Growth Hormone Proteins 0.000 claims abstract description 32
101000976075 Homo sapiens Insulin Proteins 0.000 claims abstract description 21
230000000295 complement effect Effects 0.000 claims abstract description 21
PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 claims abstract description 19
108020004414 DNA Proteins 0.000 claims description 216
238000000034 method Methods 0.000 claims description 121
239000013612 plasmid Substances 0.000 claims description 91
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 claims description 84
108090001061 Insulin Proteins 0.000 claims description 47
102000004877 Insulin Human genes 0.000 claims description 41
229940125396 insulin Drugs 0.000 claims description 41
239000000376 reactant Substances 0.000 claims description 40
102000004190 Enzymes Human genes 0.000 claims description 34
108090000790 Enzymes Proteins 0.000 claims description 34
229940088598 enzyme Drugs 0.000 claims description 34
238000006243 chemical reaction Methods 0.000 claims description 31
238000005304 joining Methods 0.000 claims description 31
239000000203 mixture Substances 0.000 claims description 28
108091008146 restriction endonucleases Proteins 0.000 claims description 28
241000588724 Escherichia coli Species 0.000 claims description 25
239000003795 chemical substances by application Substances 0.000 claims description 25
102000006382 Ribonucleases Human genes 0.000 claims description 23
108010083644 Ribonucleases Proteins 0.000 claims description 23
230000002068 genetic effect Effects 0.000 claims description 23
230000003196 chaotropic effect Effects 0.000 claims description 22
241000894006 Bacteria Species 0.000 claims description 17
102000053602 DNA Human genes 0.000 claims description 17
239000003161 ribonuclease inhibitor Substances 0.000 claims description 17
102000012410 DNA Ligases Human genes 0.000 claims description 15
108010061982 DNA Ligases Proteins 0.000 claims description 15
230000003301 hydrolyzing effect Effects 0.000 claims description 15
210000004153 islets of langerhan Anatomy 0.000 claims description 15
238000004519 manufacturing process Methods 0.000 claims description 14
108091028043 Nucleic acid sequence Proteins 0.000 claims description 13
102000002260 Alkaline Phosphatase Human genes 0.000 claims description 12
108020004774 Alkaline Phosphatase Proteins 0.000 claims description 12
ZJYYHGLJYGJLLN-UHFFFAOYSA-N guanidinium thiocyanate Chemical compound SC#N.NC(N)=N ZJYYHGLJYGJLLN-UHFFFAOYSA-N 0.000 claims description 12
210000000496 pancreas Anatomy 0.000 claims description 12
150000001450 anions Chemical class 0.000 claims description 11
150000001768 cations Chemical class 0.000 claims description 11
125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 claims description 10
210000001519 tissue Anatomy 0.000 claims description 10
108010000521 Human Growth Hormone Proteins 0.000 claims description 9
108010076181 Proinsulin Proteins 0.000 claims description 8
230000015556 catabolic process Effects 0.000 claims description 8
238000006731 degradation reaction Methods 0.000 claims description 8
230000001817 pituitary effect Effects 0.000 claims description 8
230000002194 synthesizing effect Effects 0.000 claims description 8
125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 7
102000002265 Human Growth Hormone Human genes 0.000 claims description 6
239000000854 Human Growth Hormone Substances 0.000 claims description 6
ZMZDMBWJUHKJPS-UHFFFAOYSA-M Thiocyanate anion Chemical compound [S-]C#N ZMZDMBWJUHKJPS-UHFFFAOYSA-M 0.000 claims description 6
ZMZDMBWJUHKJPS-UHFFFAOYSA-N hydrogen thiocyanate Natural products SC#N ZMZDMBWJUHKJPS-UHFFFAOYSA-N 0.000 claims description 6
230000006798 recombination Effects 0.000 claims description 6
238000005215 recombination Methods 0.000 claims description 6
125000002480 thymidyl group Chemical group 0.000 claims description 6
101100459319 Arabidopsis thaliana VIII-2 gene Proteins 0.000 claims description 5
238000006555 catalytic reaction Methods 0.000 claims description 5
ZRALSGWEFCBTJO-UHFFFAOYSA-O guanidinium Chemical compound NC(N)=[NH2+] ZRALSGWEFCBTJO-UHFFFAOYSA-O 0.000 claims description 5
101710162629 Trypsin inhibitor Proteins 0.000 claims description 4
238000002156 mixing Methods 0.000 claims description 4
101100161471 Arabidopsis thaliana ABCB24 gene Proteins 0.000 claims description 3
102100021942 C-C motif chemokine 28 Human genes 0.000 claims description 3
102100034701 Cilia- and flagella-associated protein 20 Human genes 0.000 claims description 3
102000029816 Collagenase Human genes 0.000 claims description 3
108060005980 Collagenase Proteins 0.000 claims description 3
102100023303 Germ cell-less protein-like 1 Human genes 0.000 claims description 3
101000897477 Homo sapiens C-C motif chemokine 28 Proteins 0.000 claims description 3
101000946179 Homo sapiens Cilia- and flagella-associated protein 20 Proteins 0.000 claims description 3
101000830085 Homo sapiens Germ cell-less protein-like 1 Proteins 0.000 claims description 3
101100434038 Hordeum vulgare ACL1.3 gene Proteins 0.000 claims description 3
229940122618 Trypsin inhibitor Drugs 0.000 claims description 3
229960002424 collagenase Drugs 0.000 claims description 3
210000004923 pancreatic tissue Anatomy 0.000 claims description 3
239000002753 trypsin inhibitor Substances 0.000 claims description 3
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 claims description 3
125000003275 alpha amino acid group Chemical group 0.000 claims 11
239000003153 chemical reaction reagent Substances 0.000 claims 8
DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 claims 4
102100026324 Beclin 1-associated autophagy-related key regulator Human genes 0.000 claims 2
102100032367 C-C motif chemokine 5 Human genes 0.000 claims 2
101000766227 Homo sapiens Beclin 1-associated autophagy-related key regulator Proteins 0.000 claims 2
101000797762 Homo sapiens C-C motif chemokine 5 Proteins 0.000 claims 2
229920001296 polysiloxane Polymers 0.000 claims 2
FRGKKTITADJNOE-UHFFFAOYSA-N sulfanyloxyethane Chemical compound CCOS FRGKKTITADJNOE-UHFFFAOYSA-N 0.000 claims 2
238000013518 transcription Methods 0.000 abstract description 3
230000035897 transcription Effects 0.000 abstract description 3
210000004027 cell Anatomy 0.000 description 64
235000018102 proteins Nutrition 0.000 description 51
239000012634 fragment Substances 0.000 description 27
150000001413 amino acids Chemical group 0.000 description 26
102100031780 Endonuclease Human genes 0.000 description 24
239000000047 product Substances 0.000 description 22
230000015572 biosynthetic process Effects 0.000 description 21
241000700159 Rattus Species 0.000 description 19
238000002955 isolation Methods 0.000 description 18
108010092799 RNA-directed DNA polymerase Proteins 0.000 description 15
238000003776 cleavage reaction Methods 0.000 description 15
241000282414 Homo sapiens Species 0.000 description 14
230000008569 process Effects 0.000 description 14
230000007017 scission Effects 0.000 description 14
238000003786 synthesis reaction Methods 0.000 description 13
229910019142 PO4 Inorganic materials 0.000 description 11
239000001226 triphosphate Substances 0.000 description 11
235000011178 triphosphate Nutrition 0.000 description 11
238000000605 extraction Methods 0.000 description 10
108010042407 Endonucleases Proteins 0.000 description 9
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 9
239000010452 phosphate Substances 0.000 description 9
238000000746 purification Methods 0.000 description 9
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 8
235000001014 amino acid Nutrition 0.000 description 8
229940024606 amino acid Drugs 0.000 description 8
239000003398 denaturant Substances 0.000 description 8
-1 guanylguanidinium Chemical compound 0.000 description 8
239000011541 reaction mixture Substances 0.000 description 8
125000002264 triphosphate group Chemical class [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 8
238000004587 chromatography analysis Methods 0.000 description 7
230000000694 effects Effects 0.000 description 7
235000021317 phosphate Nutrition 0.000 description 7
238000011160 research Methods 0.000 description 7
230000009466 transformation Effects 0.000 description 7
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
239000004098 Tetracycline Substances 0.000 description 6
238000012869 ethanol precipitation Methods 0.000 description 6
239000000499 gel Substances 0.000 description 6
230000012010 growth Effects 0.000 description 6
230000010076 replication Effects 0.000 description 6
229960002180 tetracycline Drugs 0.000 description 6
229930101283 tetracycline Natural products 0.000 description 6
235000019364 tetracycline Nutrition 0.000 description 6
150000003522 tetracyclines Chemical class 0.000 description 6
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 5
101710163270 Nuclease Proteins 0.000 description 5
101000868151 Rattus norvegicus Somatotropin Proteins 0.000 description 5
RWQNBRDOKXIBIV-UHFFFAOYSA-N Thymine Natural products CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 5
241000251539 Vertebrata <Metazoa> Species 0.000 description 5
238000004925 denaturation Methods 0.000 description 5
230000036425 denaturation Effects 0.000 description 5
238000001502 gel electrophoresis Methods 0.000 description 5
239000002609 medium Substances 0.000 description 5
230000003389 potentiating effect Effects 0.000 description 5
239000002243 precursor Substances 0.000 description 5
238000002360 preparation method Methods 0.000 description 5
108090000765 processed proteins & peptides Proteins 0.000 description 5
IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
108020004635 Complementary DNA Proteins 0.000 description 4
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 4
229920005654 Sephadex Polymers 0.000 description 4
239000012507 Sephadex™ Substances 0.000 description 4
239000007983 Tris buffer Substances 0.000 description 4
230000009471 action Effects 0.000 description 4
239000007795 chemical reaction product Substances 0.000 description 4
230000029087 digestion Effects 0.000 description 4
238000002474 experimental method Methods 0.000 description 4
239000000463 material Substances 0.000 description 4
229920002401 polyacrylamide Polymers 0.000 description 4
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 3
ZKHQWZAMYRWXGA-UHFFFAOYSA-N Adenosine triphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C1O ZKHQWZAMYRWXGA-UHFFFAOYSA-N 0.000 description 3
108091026890 Coding region Proteins 0.000 description 3
108010017826 DNA Polymerase I Proteins 0.000 description 3
102000004594 DNA Polymerase I Human genes 0.000 description 3
206010059866 Drug resistance Diseases 0.000 description 3
ZGTMUACCHSMWAC-UHFFFAOYSA-L EDTA disodium salt (anhydrous) Chemical compound [Na+].[Na+].OC(=O)CN(CC([O-])=O)CCN(CC(O)=O)CC([O-])=O ZGTMUACCHSMWAC-UHFFFAOYSA-L 0.000 description 3
WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 3
229910003873 O—P—O Inorganic materials 0.000 description 3
238000012300 Sequence Analysis Methods 0.000 description 3
108020004682 Single-Stranded DNA Proteins 0.000 description 3
108020004566 Transfer RNA Proteins 0.000 description 3
230000001154 acute effect Effects 0.000 description 3
KOSRFJWDECSPRO-UHFFFAOYSA-N alpha-L-glutamyl-L-glutamic acid Natural products OC(=O)CCC(N)C(=O)NC(CCC(O)=O)C(O)=O KOSRFJWDECSPRO-UHFFFAOYSA-N 0.000 description 3
229960000723 ampicillin Drugs 0.000 description 3
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 3
230000008901 benefit Effects 0.000 description 3
238000010804 cDNA synthesis Methods 0.000 description 3
AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 3
230000001413 cellular effect Effects 0.000 description 3
238000005119 centrifugation Methods 0.000 description 3
238000012512 characterization method Methods 0.000 description 3
SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 3
SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 3
RGWHQCVHVJXOKC-SHYZEUOFSA-N dCTP Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](CO[P@](O)(=O)O[P@](O)(=O)OP(O)(O)=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-N 0.000 description 3
HAAZLUGHYHWQIW-KVQBGUIXSA-N dGTP Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 HAAZLUGHYHWQIW-KVQBGUIXSA-N 0.000 description 3
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 3
239000003814 drug Substances 0.000 description 3
238000001962 electrophoresis Methods 0.000 description 3
229940088597 hormone Drugs 0.000 description 3
239000005556 hormone Substances 0.000 description 3
238000011534 incubation Methods 0.000 description 3
238000003780 insertion Methods 0.000 description 3
230000037431 insertion Effects 0.000 description 3
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 3
102000040430 polynucleotide Human genes 0.000 description 3
108091033319 polynucleotide Proteins 0.000 description 3
239000002157 polynucleotide Substances 0.000 description 3
239000002244 precipitate Substances 0.000 description 3
108010066381 preproinsulin Proteins 0.000 description 3
239000012266 salt solution Substances 0.000 description 3
238000000926 separation method Methods 0.000 description 3
239000000243 solution Substances 0.000 description 3
241000894007 species Species 0.000 description 3
229940113082 thymine Drugs 0.000 description 3
238000013519 translation Methods 0.000 description 3
KDCGOANMDULRCW-UHFFFAOYSA-N 7H-purine Chemical compound N1=CNC2=NC=NC2=C1 KDCGOANMDULRCW-UHFFFAOYSA-N 0.000 description 2
DWOGMPWRQQWPPF-GUBZILKMSA-N Asp-Leu-Glu Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(O)=O DWOGMPWRQQWPPF-GUBZILKMSA-N 0.000 description 2
241000713838 Avian myeloblastosis virus Species 0.000 description 2
108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
108010071230 GCGC-specific type II deoxyribonucleases Proteins 0.000 description 2
XZUUUKNKNWVPHQ-JYJNAYRXSA-N Gln-Phe-Leu Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC(C)C)C(O)=O XZUUUKNKNWVPHQ-JYJNAYRXSA-N 0.000 description 2
CUXJIASLBRJOFV-LAEOZQHASA-N Glu-Gly-Ile Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H]([C@@H](C)CC)C(O)=O CUXJIASLBRJOFV-LAEOZQHASA-N 0.000 description 2
ABPRMMYHROQBLY-NKWVEPMBSA-N Gly-Ser-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CO)NC(=O)CN)C(=O)O ABPRMMYHROQBLY-NKWVEPMBSA-N 0.000 description 2
239000012981 Hank's balanced salt solution Substances 0.000 description 2
241000282412 Homo Species 0.000 description 2
101500025353 Homo sapiens Insulin A chain Proteins 0.000 description 2
101500025354 Homo sapiens Insulin B chain Proteins 0.000 description 2
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
108091026898 Leader sequence (mRNA) Proteins 0.000 description 2
HFBCHNRFRYLZNV-GUBZILKMSA-N Leu-Glu-Asp Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O HFBCHNRFRYLZNV-GUBZILKMSA-N 0.000 description 2
AUBMZAMQCOYSIC-MNXVOIDGSA-N Leu-Ile-Gln Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(O)=O AUBMZAMQCOYSIC-MNXVOIDGSA-N 0.000 description 2
LXKNSJLSGPNHSK-KKUMJFAQSA-N Leu-Leu-Lys Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)O)N LXKNSJLSGPNHSK-KKUMJFAQSA-N 0.000 description 2
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
108091034117 Oligonucleotide Proteins 0.000 description 2
102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 2
108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 2
208000007913 Pituitary Neoplasms Diseases 0.000 description 2
108091006629 SLC13A2 Proteins 0.000 description 2
240000004808 Saccharomyces cerevisiae Species 0.000 description 2
FVFUOQIYDPAIJR-XIRDDKMYSA-N Ser-Trp-Leu Chemical compound CC(C)C[C@@H](C(=O)O)NC(=O)[C@H](CC1=CNC2=CC=CC=C21)NC(=O)[C@H](CO)N FVFUOQIYDPAIJR-XIRDDKMYSA-N 0.000 description 2
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 2
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
229930006000 Sucrose Natural products 0.000 description 2
CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 2
241000282898 Sus scrofa Species 0.000 description 2
RZCIEJXAILMSQK-JXOAFFINSA-N TTP Chemical compound O=C1NC(=O)C(C)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 RZCIEJXAILMSQK-JXOAFFINSA-N 0.000 description 2
ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical compound O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 description 2
239000002253 acid Substances 0.000 description 2
238000005904 alkaline hydrolysis reaction Methods 0.000 description 2
238000004458 analytical method Methods 0.000 description 2
239000012736 aqueous medium Substances 0.000 description 2
235000015278 beef Nutrition 0.000 description 2
239000000872 buffer Substances 0.000 description 2
230000032823 cell division Effects 0.000 description 2
239000002131 composite material Substances 0.000 description 2
238000011109 contamination Methods 0.000 description 2
210000004748 cultured cell Anatomy 0.000 description 2
235000018417 cysteine Nutrition 0.000 description 2
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
239000005549 deoxyribonucleoside Substances 0.000 description 2
230000001419 dependent effect Effects 0.000 description 2
206010012601 diabetes mellitus Diseases 0.000 description 2
229940079593 drug Drugs 0.000 description 2
238000005516 engineering process Methods 0.000 description 2
239000000284 extract Substances 0.000 description 2
108010055341 glutamyl-glutamic acid Proteins 0.000 description 2
108010010147 glycylglutamine Proteins 0.000 description 2
230000007062 hydrolysis Effects 0.000 description 2
238000006460 hydrolysis reaction Methods 0.000 description 2
125000002887 hydroxy group Chemical group [H]O* 0.000 description 2
238000007169 ligase reaction Methods 0.000 description 2
239000007788 liquid Substances 0.000 description 2
MJJFTDMZSMPNCL-UHFFFAOYSA-M lithium;2-hydroxy-3,4-diiodobenzoate Chemical compound [Li+].OC1=C(I)C(I)=CC=C1C([O-])=O MJJFTDMZSMPNCL-UHFFFAOYSA-M 0.000 description 2
229910001629 magnesium chloride Inorganic materials 0.000 description 2
239000003550 marker Substances 0.000 description 2
230000004060 metabolic process Effects 0.000 description 2
230000000813 microbial effect Effects 0.000 description 2
229910052757 nitrogen Inorganic materials 0.000 description 2
239000002777 nucleoside Substances 0.000 description 2
229940046166 oligodeoxynucleotide Drugs 0.000 description 2
239000008188 pellet Substances 0.000 description 2
239000000813 peptide hormone Substances 0.000 description 2
150000003013 phosphoric acid derivatives Chemical group 0.000 description 2
102000004196 processed proteins & peptides Human genes 0.000 description 2
230000002285 radioactive effect Effects 0.000 description 2
230000002441 reversible effect Effects 0.000 description 2
150000003839 salts Chemical class 0.000 description 2
238000007086 side reaction Methods 0.000 description 2
239000001632 sodium acetate Substances 0.000 description 2
235000017281 sodium acetate Nutrition 0.000 description 2
239000000126 substance Substances 0.000 description 2
239000005720 sucrose Substances 0.000 description 2
239000000725 suspension Substances 0.000 description 2
125000003396 thiol group Chemical group [H]S* 0.000 description 2
230000003612 virological effect Effects 0.000 description 2
239000011800 void material Substances 0.000 description 2
GMKMEZVLHJARHF-UHFFFAOYSA-N (2R,6R)-form-2.6-Diaminoheptanedioic acid Natural products OC(=O)C(N)CCCC(N)C(O)=O GMKMEZVLHJARHF-UHFFFAOYSA-N 0.000 description 1
ASJSAQIRZKANQN-CRCLSJGQSA-N 2-deoxy-D-ribose Chemical compound OC[C@@H](O)[C@@H](O)CC=O ASJSAQIRZKANQN-CRCLSJGQSA-N 0.000 description 1
DYIFXNDAYPEXGI-UHFFFAOYSA-N 2-hydroxy-3,4-diiodobenzoic acid Chemical compound OC(=O)C1=CC=C(I)C(I)=C1O DYIFXNDAYPEXGI-UHFFFAOYSA-N 0.000 description 1
QCQCHGYLTSGIGX-GHXANHINSA-N 4-[[(3ar,5ar,5br,7ar,9s,11ar,11br,13as)-5a,5b,8,8,11a-pentamethyl-3a-[(5-methylpyridine-3-carbonyl)amino]-2-oxo-1-propan-2-yl-4,5,6,7,7a,9,10,11,11b,12,13,13a-dodecahydro-3h-cyclopenta[a]chrysen-9-yl]oxy]-2,2-dimethyl-4-oxobutanoic acid Chemical compound N([C@@]12CC[C@@]3(C)[C@]4(C)CC[C@H]5C(C)(C)[C@@H](OC(=O)CC(C)(C)C(O)=O)CC[C@]5(C)[C@H]4CC[C@@H]3C1=C(C(C2)=O)C(C)C)C(=O)C1=CN=CC(C)=C1 QCQCHGYLTSGIGX-GHXANHINSA-N 0.000 description 1
229930024421 Adenine Natural products 0.000 description 1
229920001817 Agar Polymers 0.000 description 1
BTYTYHBSJKQBQA-GCJQMDKQSA-N Ala-Asp-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](C)N)O BTYTYHBSJKQBQA-GCJQMDKQSA-N 0.000 description 1
RXTBLQVXNIECFP-FXQIFTODSA-N Ala-Gln-Gln Chemical compound C[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(O)=O RXTBLQVXNIECFP-FXQIFTODSA-N 0.000 description 1
OQCPATDFWYYDDX-HGNGGELXSA-N Ala-Gln-His Chemical compound C[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](Cc1cnc[nH]1)C(O)=O OQCPATDFWYYDDX-HGNGGELXSA-N 0.000 description 1
OYJCVIGKMXUVKB-GARJFASQSA-N Ala-Leu-Pro Chemical compound C[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@@H]1C(=O)O)N OYJCVIGKMXUVKB-GARJFASQSA-N 0.000 description 1
DEWWPUNXRNGMQN-LPEHRKFASA-N Ala-Met-Pro Chemical compound C[C@@H](C(=O)N[C@@H](CCSC)C(=O)N1CCC[C@@H]1C(=O)O)N DEWWPUNXRNGMQN-LPEHRKFASA-N 0.000 description 1
BDQNLQSWRAPHGU-DLOVCJGASA-N Ala-Phe-Cys Chemical compound C[C@@H](C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CS)C(=O)O)N BDQNLQSWRAPHGU-DLOVCJGASA-N 0.000 description 1
GCTANJIJJROSLH-GVARAGBVSA-N Ala-Tyr-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H](CC1=CC=C(C=C1)O)NC(=O)[C@H](C)N GCTANJIJJROSLH-GVARAGBVSA-N 0.000 description 1
USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
239000005695 Ammonium acetate Substances 0.000 description 1
UAOSDDXCTBIPCA-QXEWZRGKSA-N Arg-Ile-Gly Chemical compound CC[C@H](C)[C@@H](C(=O)NCC(=O)O)NC(=O)[C@H](CCCN=C(N)N)N UAOSDDXCTBIPCA-QXEWZRGKSA-N 0.000 description 1
GXXWTNKNFFKTJB-NAKRPEOUSA-N Arg-Ile-Ser Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CO)C(O)=O GXXWTNKNFFKTJB-NAKRPEOUSA-N 0.000 description 1
MJINRRBEMOLJAK-DCAQKATOSA-N Arg-Lys-Asp Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CCCN=C(N)N MJINRRBEMOLJAK-DCAQKATOSA-N 0.000 description 1
OQPAZKMGCWPERI-GUBZILKMSA-N Arg-Ser-Val Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(O)=O OQPAZKMGCWPERI-GUBZILKMSA-N 0.000 description 1
WCZXPVPHUMYLMS-VEVYYDQMSA-N Arg-Thr-Asp Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(O)=O WCZXPVPHUMYLMS-VEVYYDQMSA-N 0.000 description 1
UZSQXCMNUPKLCC-FJXKBIBVSA-N Arg-Thr-Gly Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(O)=O UZSQXCMNUPKLCC-FJXKBIBVSA-N 0.000 description 1
OGZBJJLRKQZRHL-KJEVXHAQSA-N Arg-Thr-Tyr Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H]([C@H](O)C)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 OGZBJJLRKQZRHL-KJEVXHAQSA-N 0.000 description 1
239000004475 Arginine Substances 0.000 description 1
PDQBXRSOSCTGKY-ACZMJKKPSA-N Asn-Ala-Gln Chemical compound C[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)O)NC(=O)[C@H](CC(=O)N)N PDQBXRSOSCTGKY-ACZMJKKPSA-N 0.000 description 1
QEYJFBMTSMLPKZ-ZKWXMUAHSA-N Asn-Ala-Val Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(O)=O QEYJFBMTSMLPKZ-ZKWXMUAHSA-N 0.000 description 1
NCFJQJRLQJEECD-NHCYSSNCSA-N Asn-Leu-Val Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(O)=O NCFJQJRLQJEECD-NHCYSSNCSA-N 0.000 description 1
ICDDSTLEMLGSTB-GUBZILKMSA-N Asn-Met-Arg Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O ICDDSTLEMLGSTB-GUBZILKMSA-N 0.000 description 1
YSYTWUMRHSFODC-QWRGUYRKSA-N Asn-Tyr-Gly Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)NCC(O)=O YSYTWUMRHSFODC-QWRGUYRKSA-N 0.000 description 1
XXAMCEGRCZQGEM-ZLUOBGJFSA-N Asp-Ser-Asn Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(O)=O XXAMCEGRCZQGEM-ZLUOBGJFSA-N 0.000 description 1
UTLCRGFJFSZWAW-OLHMAJIHSA-N Asp-Thr-Asn Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)O)NC(=O)[C@H](CC(=O)O)N)O UTLCRGFJFSZWAW-OLHMAJIHSA-N 0.000 description 1
DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
240000006439 Aspergillus oryzae Species 0.000 description 1
235000002247 Aspergillus oryzae Nutrition 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
241000208199 Buxus sempervirens Species 0.000 description 1
108010075254 C-Peptide Proteins 0.000 description 1
101100385576 Caenorhabditis elegans ctg-1 gene Proteins 0.000 description 1
241000195493 Cryptophyta Species 0.000 description 1
UKVGHFORADMBEN-GUBZILKMSA-N Cys-Arg-Arg Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O UKVGHFORADMBEN-GUBZILKMSA-N 0.000 description 1
IDZDFWJNPOOOHE-KKUMJFAQSA-N Cys-Phe-Lys Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CCCCN)C(=O)O)NC(=O)[C@H](CS)N IDZDFWJNPOOOHE-KKUMJFAQSA-N 0.000 description 1
CHRCKSPMGYDLIA-SRVKXCTJSA-N Cys-Phe-Ser Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CO)C(O)=O CHRCKSPMGYDLIA-SRVKXCTJSA-N 0.000 description 1
HMFHBZSHGGEWLO-SOOFDHNKSA-N D-ribofuranose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H]1O HMFHBZSHGGEWLO-SOOFDHNKSA-N 0.000 description 1
208000027219 Deficiency disease Diseases 0.000 description 1
BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
241000196324 Embryophyta Species 0.000 description 1
101900234631 Escherichia coli DNA polymerase I Proteins 0.000 description 1
108060002716 Exonuclease Proteins 0.000 description 1
241000233866 Fungi Species 0.000 description 1
108010012003 GGCC-specific type II deoxyribonucleases Proteins 0.000 description 1
KVYVOGYEMPEXBT-GUBZILKMSA-N Gln-Ala-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCC(N)=O KVYVOGYEMPEXBT-GUBZILKMSA-N 0.000 description 1
MQANCSUBSBJNLU-KKUMJFAQSA-N Gln-Arg-Tyr Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O MQANCSUBSBJNLU-KKUMJFAQSA-N 0.000 description 1
MADFVRSKEIEZHZ-DCAQKATOSA-N Gln-Gln-Lys Chemical compound C(CCN)C[C@@H](C(=O)O)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H](CCC(=O)N)N MADFVRSKEIEZHZ-DCAQKATOSA-N 0.000 description 1
LFIVHGMKWFGUGK-IHRRRGAJSA-N Gln-Glu-Phe Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)N)N LFIVHGMKWFGUGK-IHRRRGAJSA-N 0.000 description 1
FTIJVMLAGRAYMJ-MNXVOIDGSA-N Gln-Ile-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H](N)CCC(N)=O FTIJVMLAGRAYMJ-MNXVOIDGSA-N 0.000 description 1
NHMRJKKAVMENKJ-WDCWCFNPSA-N Gln-Thr-Leu Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(C)C)C(O)=O NHMRJKKAVMENKJ-WDCWCFNPSA-N 0.000 description 1
XKPACHRGOWQHFH-IRIUXVKKSA-N Gln-Thr-Tyr Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O XKPACHRGOWQHFH-IRIUXVKKSA-N 0.000 description 1
UTKUTMJSWKKHEM-WDSKDSINSA-N Glu-Ala-Gly Chemical compound OC(=O)CNC(=O)[C@H](C)NC(=O)[C@@H](N)CCC(O)=O UTKUTMJSWKKHEM-WDSKDSINSA-N 0.000 description 1
PHONAZGUEGIOEM-GLLZPBPUSA-N Glu-Glu-Thr Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O PHONAZGUEGIOEM-GLLZPBPUSA-N 0.000 description 1
WTMZXOPHTIVFCP-QEWYBTABSA-N Glu-Ile-Phe Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 WTMZXOPHTIVFCP-QEWYBTABSA-N 0.000 description 1
MWMJCGBSIORNCD-AVGNSLFASA-N Glu-Leu-Leu Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O MWMJCGBSIORNCD-AVGNSLFASA-N 0.000 description 1
NNQDRRUXFJYCCJ-NHCYSSNCSA-N Glu-Pro-Val Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C(C)C)C(O)=O NNQDRRUXFJYCCJ-NHCYSSNCSA-N 0.000 description 1
SYAYROHMAIHWFB-KBIXCLLPSA-N Glu-Ser-Ile Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O SYAYROHMAIHWFB-KBIXCLLPSA-N 0.000 description 1
LJPIRKICOISLKN-WHFBIAKZSA-N Gly-Ala-Ser Chemical compound NCC(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(O)=O LJPIRKICOISLKN-WHFBIAKZSA-N 0.000 description 1
UHPAZODVFFYEEL-QWRGUYRKSA-N Gly-Leu-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)CN UHPAZODVFFYEEL-QWRGUYRKSA-N 0.000 description 1
BMWFDYIYBAFROD-WPRPVWTQSA-N Gly-Pro-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)CN BMWFDYIYBAFROD-WPRPVWTQSA-N 0.000 description 1
239000004471 Glycine Substances 0.000 description 1
244000068988 Glycine max Species 0.000 description 1
235000010469 Glycine max Nutrition 0.000 description 1
UYTPUPDQBNUYGX-UHFFFAOYSA-N Guanine Natural products O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 1
SQSPRWMERUQXNE-UHFFFAOYSA-N Guanylurea Chemical compound NC(=N)NC(N)=O SQSPRWMERUQXNE-UHFFFAOYSA-N 0.000 description 1
JBCLFWXMTIKCCB-UHFFFAOYSA-N H-Gly-Phe-OH Natural products NCC(=O)NC(C(O)=O)CC1=CC=CC=C1 JBCLFWXMTIKCCB-UHFFFAOYSA-N 0.000 description 1
241000606768 Haemophilus influenzae Species 0.000 description 1
241000238631 Hexapoda Species 0.000 description 1
VOEGKUNRHYKYSU-XVYDVKMFSA-N His-Asp-Ala Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C)C(O)=O VOEGKUNRHYKYSU-XVYDVKMFSA-N 0.000 description 1
PGRPSOUCWRBWKZ-DLOVCJGASA-N His-Lys-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CC1=CN=CN1 PGRPSOUCWRBWKZ-DLOVCJGASA-N 0.000 description 1
108090000144 Human Proteins Proteins 0.000 description 1
102000003839 Human Proteins Human genes 0.000 description 1
206010020751 Hypersensitivity Diseases 0.000 description 1
IITVUURPOYGCTD-NAKRPEOUSA-N Ile-Pro-Ala Chemical compound CC[C@H](C)[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(O)=O IITVUURPOYGCTD-NAKRPEOUSA-N 0.000 description 1
HGCNKOLVKRAVHD-UHFFFAOYSA-N L-Met-L-Phe Natural products CSCCC(N)C(=O)NC(C(O)=O)CC1=CC=CC=C1 HGCNKOLVKRAVHD-UHFFFAOYSA-N 0.000 description 1
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
UILIPCLTHRPCRB-XUXIUFHCSA-N Leu-Arg-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(C)C)N UILIPCLTHRPCRB-XUXIUFHCSA-N 0.000 description 1
VKOAHIRLIUESLU-ULQDDVLXSA-N Leu-Arg-Phe Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O VKOAHIRLIUESLU-ULQDDVLXSA-N 0.000 description 1
PPBKJAQJAUHZKX-SRVKXCTJSA-N Leu-Cys-Leu Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CS)C(=O)N[C@H](C(O)=O)CC(C)C PPBKJAQJAUHZKX-SRVKXCTJSA-N 0.000 description 1
DLCXCECTCPKKCD-GUBZILKMSA-N Leu-Gln-Asn Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O DLCXCECTCPKKCD-GUBZILKMSA-N 0.000 description 1
BKTXKJMNTSMJDQ-AVGNSLFASA-N Leu-His-Gln Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H](CCC(=O)N)C(=O)O)N BKTXKJMNTSMJDQ-AVGNSLFASA-N 0.000 description 1
RXGLHDWAZQECBI-SRVKXCTJSA-N Leu-Leu-Ser Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(O)=O RXGLHDWAZQECBI-SRVKXCTJSA-N 0.000 description 1
IEWBEPKLKUXQBU-VOAKCMCISA-N Leu-Leu-Thr Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(O)=O IEWBEPKLKUXQBU-VOAKCMCISA-N 0.000 description 1
ZDBMWELMUCLUPL-QEJZJMRPSA-N Leu-Phe-Ala Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(=O)N[C@@H](C)C(O)=O)CC1=CC=CC=C1 ZDBMWELMUCLUPL-QEJZJMRPSA-N 0.000 description 1
BRTVHXHCUSXYRI-CIUDSAMLSA-N Leu-Ser-Ser Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(O)=O BRTVHXHCUSXYRI-CIUDSAMLSA-N 0.000 description 1
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
102000003960 Ligases Human genes 0.000 description 1
108090000364 Ligases Proteins 0.000 description 1
108090001060 Lipase Proteins 0.000 description 1
102000004882 Lipase Human genes 0.000 description 1
239000004367 Lipase Substances 0.000 description 1
WHXSMMKQMYFTQS-UHFFFAOYSA-N Lithium Chemical compound [Li] WHXSMMKQMYFTQS-UHFFFAOYSA-N 0.000 description 1
PXHCFKXNSBJSTQ-KKUMJFAQSA-N Lys-Asn-Tyr Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CCCCN)N)O PXHCFKXNSBJSTQ-KKUMJFAQSA-N 0.000 description 1
IWWMPCPLFXFBAF-SRVKXCTJSA-N Lys-Asp-Leu Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(O)=O IWWMPCPLFXFBAF-SRVKXCTJSA-N 0.000 description 1
PBIPLDMFHAICIP-DCAQKATOSA-N Lys-Glu-Glu Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O PBIPLDMFHAICIP-DCAQKATOSA-N 0.000 description 1
RBEATVHTWHTHTJ-KKUMJFAQSA-N Lys-Leu-Lys Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(O)=O RBEATVHTWHTHTJ-KKUMJFAQSA-N 0.000 description 1
239000004472 Lysine Substances 0.000 description 1
241000124008 Mammalia Species 0.000 description 1
YRAWWKUTNBILNT-FXQIFTODSA-N Met-Ala-Ala Chemical compound CSCC[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(O)=O YRAWWKUTNBILNT-FXQIFTODSA-N 0.000 description 1
WGBMNLCRYKSWAR-DCAQKATOSA-N Met-Asp-Lys Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN WGBMNLCRYKSWAR-DCAQKATOSA-N 0.000 description 1
FWTBMGAKKPSTBT-GUBZILKMSA-N Met-Gln-Glu Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O FWTBMGAKKPSTBT-GUBZILKMSA-N 0.000 description 1
SJDQOYTYNGZZJX-SRVKXCTJSA-N Met-Glu-Leu Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(O)=O SJDQOYTYNGZZJX-SRVKXCTJSA-N 0.000 description 1
FYRUJIJAUPHUNB-IUCAKERBSA-N Met-Gly-Arg Chemical compound CSCC[C@H](N)C(=O)NCC(=O)N[C@H](C(O)=O)CCCNC(N)=N FYRUJIJAUPHUNB-IUCAKERBSA-N 0.000 description 1
241000237852 Mollusca Species 0.000 description 1
YBAFDPFAUTYYRW-UHFFFAOYSA-N N-L-alpha-glutamyl-L-leucine Natural products CC(C)CC(C(O)=O)NC(=O)C(N)CCC(O)=O YBAFDPFAUTYYRW-UHFFFAOYSA-N 0.000 description 1
XZFYRXDAULDNFX-UHFFFAOYSA-N N-L-cysteinyl-L-phenylalanine Natural products SCC(N)C(=O)NC(C(O)=O)CC1=CC=CC=C1 XZFYRXDAULDNFX-UHFFFAOYSA-N 0.000 description 1
XMBSYZWANAQXEV-UHFFFAOYSA-N N-alpha-L-glutamyl-L-phenylalanine Natural products OC(=O)CCC(N)C(=O)NC(C(O)=O)CC1=CC=CC=C1 XMBSYZWANAQXEV-UHFFFAOYSA-N 0.000 description 1
101100205189 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) leu-5 gene Proteins 0.000 description 1
108010067035 Pancrelipase Proteins 0.000 description 1
102000015731 Peptide Hormones Human genes 0.000 description 1
108010038988 Peptide Hormones Proteins 0.000 description 1
WSXKXSBOJXEZDV-DLOVCJGASA-N Phe-Ala-Asn Chemical compound NC(=O)C[C@@H](C([O-])=O)NC(=O)[C@H](C)NC(=O)[C@@H]([NH3+])CC1=CC=CC=C1 WSXKXSBOJXEZDV-DLOVCJGASA-N 0.000 description 1
CYZBFPYMSJGBRL-DRZSPHRISA-N Phe-Ala-Glu Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(O)=O CYZBFPYMSJGBRL-DRZSPHRISA-N 0.000 description 1
LDSOBEJVGGVWGD-DLOVCJGASA-N Phe-Asp-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](N)CC1=CC=CC=C1 LDSOBEJVGGVWGD-DLOVCJGASA-N 0.000 description 1
HOYQLNNGMHXZDW-KKUMJFAQSA-N Phe-Glu-Arg Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O HOYQLNNGMHXZDW-KKUMJFAQSA-N 0.000 description 1
QPVFUAUFEBPIPT-CDMKHQONSA-N Phe-Gly-Thr Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(O)=O QPVFUAUFEBPIPT-CDMKHQONSA-N 0.000 description 1
UNBFGVQVQGXXCK-KKUMJFAQSA-N Phe-Ser-Leu Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(O)=O UNBFGVQVQGXXCK-KKUMJFAQSA-N 0.000 description 1
JHSRGEODDALISP-XVSYOHENSA-N Phe-Thr-Asn Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(O)=O JHSRGEODDALISP-XVSYOHENSA-N 0.000 description 1
108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 1
102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 1
241000288906 Primates Species 0.000 description 1
NMELOOXSGDRBRU-YUMQZZPRSA-N Pro-Glu-Gly Chemical compound OC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H]1CCCN1 NMELOOXSGDRBRU-YUMQZZPRSA-N 0.000 description 1
DCHQYSOGURGJST-FJXKBIBVSA-N Pro-Thr-Gly Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(O)=O DCHQYSOGURGJST-FJXKBIBVSA-N 0.000 description 1
AIOWVDNPESPXRB-YTWAJWBKSA-N Pro-Thr-Pro Chemical compound C[C@H]([C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@@H]2CCCN2)O AIOWVDNPESPXRB-YTWAJWBKSA-N 0.000 description 1
ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
CZPWVGJYEJSRLH-UHFFFAOYSA-N Pyrimidine Chemical compound C1=CN=CN=C1 CZPWVGJYEJSRLH-UHFFFAOYSA-N 0.000 description 1
108010003201 RGH 0205 Proteins 0.000 description 1
108091034057 RNA (poly(A)) Proteins 0.000 description 1
108091030071 RNAI Proteins 0.000 description 1
108091028664 Ribonucleotide Proteins 0.000 description 1
PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 description 1
KYKKKSWGEPFUMR-NAKRPEOUSA-N Ser-Arg-Ile Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O KYKKKSWGEPFUMR-NAKRPEOUSA-N 0.000 description 1
FIDMVVBUOCMMJG-CIUDSAMLSA-N Ser-Asn-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](N)CO FIDMVVBUOCMMJG-CIUDSAMLSA-N 0.000 description 1
CNIIKZQXBBQHCX-FXQIFTODSA-N Ser-Asp-Arg Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O CNIIKZQXBBQHCX-FXQIFTODSA-N 0.000 description 1
MESDJCNHLZBMEP-ZLUOBGJFSA-N Ser-Asp-Asp Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O MESDJCNHLZBMEP-ZLUOBGJFSA-N 0.000 description 1
RNFKSBPHLTZHLU-WHFBIAKZSA-N Ser-Cys-Gly Chemical compound C([C@@H](C(=O)N[C@@H](CS)C(=O)NCC(=O)O)N)O RNFKSBPHLTZHLU-WHFBIAKZSA-N 0.000 description 1
GZBKRJVCRMZAST-XKBZYTNZSA-N Ser-Glu-Thr Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O GZBKRJVCRMZAST-XKBZYTNZSA-N 0.000 description 1
RJHJPZQOMKCSTP-CIUDSAMLSA-N Ser-His-Asn Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(N)=O)C(O)=O RJHJPZQOMKCSTP-CIUDSAMLSA-N 0.000 description 1
CJINPXGSKSZQNE-KBIXCLLPSA-N Ser-Ile-Gln Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(O)=O CJINPXGSKSZQNE-KBIXCLLPSA-N 0.000 description 1
VMLONWHIORGALA-SRVKXCTJSA-N Ser-Leu-Leu Chemical compound CC(C)C[C@@H](C([O-])=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]([NH3+])CO VMLONWHIORGALA-SRVKXCTJSA-N 0.000 description 1
XXNYYSXNXCJYKX-DCAQKATOSA-N Ser-Leu-Met Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(O)=O XXNYYSXNXCJYKX-DCAQKATOSA-N 0.000 description 1
WGDYNRCOQRERLZ-KKUMJFAQSA-N Ser-Lys-Phe Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)N WGDYNRCOQRERLZ-KKUMJFAQSA-N 0.000 description 1
VFWQQZMRKFOGLE-ZLUOBGJFSA-N Ser-Ser-Cys Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CS)C(=O)O)N)O VFWQQZMRKFOGLE-ZLUOBGJFSA-N 0.000 description 1
101000993800 Sus scrofa Insulin Proteins 0.000 description 1
IWAVRIPRTCJAQO-HSHDSVGOSA-N Thr-Pro-Trp Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(O)=O IWAVRIPRTCJAQO-HSHDSVGOSA-N 0.000 description 1
AHERARIZBPOMNU-KATARQTJSA-N Thr-Ser-Leu Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(O)=O AHERARIZBPOMNU-KATARQTJSA-N 0.000 description 1
BZTSQFWJNJYZSX-JRQIVUDYSA-N Thr-Tyr-Asp Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(O)=O)C(O)=O BZTSQFWJNJYZSX-JRQIVUDYSA-N 0.000 description 1
AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
239000004473 Threonine Substances 0.000 description 1
AUYYCJSJGJYCDS-LBPRGKRZSA-N Thyrolar Chemical compound IC1=CC(C[C@H](N)C(O)=O)=CC(I)=C1OC1=CC=C(O)C(I)=C1 AUYYCJSJGJYCDS-LBPRGKRZSA-N 0.000 description 1
ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 1
241000209140 Triticum Species 0.000 description 1
235000021307 Triticum Nutrition 0.000 description 1
BIBZRFIKOLGWFQ-XIRDDKMYSA-N Trp-Pro-Gln Chemical compound C1C[C@H](N(C1)C(=O)[C@H](CC2=CNC3=CC=CC=C32)N)C(=O)N[C@@H](CCC(=O)N)C(=O)O BIBZRFIKOLGWFQ-XIRDDKMYSA-N 0.000 description 1
QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
BVDHHLMIZFCAAU-BZSNNMDCSA-N Tyr-Cys-Phe Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O BVDHHLMIZFCAAU-BZSNNMDCSA-N 0.000 description 1
QSFJHIRIHOJRKS-ULQDDVLXSA-N Tyr-Leu-Arg Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O QSFJHIRIHOJRKS-ULQDDVLXSA-N 0.000 description 1
JLKVWTICWVWGSK-JYJNAYRXSA-N Tyr-Lys-Glu Chemical compound OC(=O)CC[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 JLKVWTICWVWGSK-JYJNAYRXSA-N 0.000 description 1
HRHYJNLMIJWGLF-BZSNNMDCSA-N Tyr-Ser-Phe Chemical compound C([C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=C(O)C=C1 HRHYJNLMIJWGLF-BZSNNMDCSA-N 0.000 description 1
LMSBRIVOCYOKMU-NRPADANISA-N Val-Gln-Cys Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CS)C(=O)O)N LMSBRIVOCYOKMU-NRPADANISA-N 0.000 description 1
VVZDBPBZHLQPPB-XVKPBYJWSA-N Val-Glu-Gly Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(O)=O VVZDBPBZHLQPPB-XVKPBYJWSA-N 0.000 description 1
XWYUBUYQMOUFRQ-IFFSRLJSSA-N Val-Glu-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C(C)C)N)O XWYUBUYQMOUFRQ-IFFSRLJSSA-N 0.000 description 1
UEPLNXPLHJUYPT-AVGNSLFASA-N Val-Met-Lys Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(O)=O UEPLNXPLHJUYPT-AVGNSLFASA-N 0.000 description 1
VTIAEOKFUJJBTC-YDHLFZDLSA-N Val-Tyr-Asp Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)N[C@@H](CC(=O)O)C(=O)O)N VTIAEOKFUJJBTC-YDHLFZDLSA-N 0.000 description 1
PFMSJVIPEZMKSC-DZKIICNBSA-N Val-Tyr-Glu Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)N[C@@H](CCC(=O)O)C(=O)O)N PFMSJVIPEZMKSC-DZKIICNBSA-N 0.000 description 1
KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Chemical compound CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
241000700605 Viruses Species 0.000 description 1
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
CTCBPRXHVPZNHB-VQFZJOCSSA-N [[(2r,3s,4r,5r)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate;(2r,3r,4s,5r)-2-(6-aminopurin-9-yl)-5-(hydroxymethyl)oxolane-3,4-diol Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O.C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O CTCBPRXHVPZNHB-VQFZJOCSSA-N 0.000 description 1
150000007513 acids Chemical class 0.000 description 1
229960000643 adenine Drugs 0.000 description 1
239000008272 agar Substances 0.000 description 1
235000004279 alanine Nutrition 0.000 description 1
108010005233 alanylglutamic acid Proteins 0.000 description 1
108010087924 alanylproline Proteins 0.000 description 1
208000030961 allergic reaction Diseases 0.000 description 1
HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 description 1
125000003277 amino group Chemical group 0.000 description 1
229940043376 ammonium acetate Drugs 0.000 description 1
235000019257 ammonium acetate Nutrition 0.000 description 1
230000002942 anti-growth Effects 0.000 description 1
238000013459 approach Methods 0.000 description 1
239000008346 aqueous phase Substances 0.000 description 1
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
238000010420 art technique Methods 0.000 description 1
235000009582 asparagine Nutrition 0.000 description 1
229960001230 asparagine Drugs 0.000 description 1
108010077245 asparaginyl-proline Proteins 0.000 description 1
235000003704 aspartic acid Nutrition 0.000 description 1
108010092854 aspartyllysine Proteins 0.000 description 1
230000003190 augmentative effect Effects 0.000 description 1
238000000376 autoradiography Methods 0.000 description 1
230000001580 bacterial effect Effects 0.000 description 1
OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
230000031018 biological processes and functions Effects 0.000 description 1
229940041514 candida albicans extract Drugs 0.000 description 1
230000010261 cell growth Effects 0.000 description 1
210000000170 cell membrane Anatomy 0.000 description 1
239000006285 cell suspension Substances 0.000 description 1
239000001913 cellulose Substances 0.000 description 1
229920002678 cellulose Polymers 0.000 description 1
230000008859 change Effects 0.000 description 1
229960005091 chloramphenicol Drugs 0.000 description 1
WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
210000000349 chromosome Anatomy 0.000 description 1
230000001684 chronic effect Effects 0.000 description 1
238000010367 cloning Methods 0.000 description 1
238000004440 column chromatography Methods 0.000 description 1
238000010276 construction Methods 0.000 description 1
230000001276 controlling effect Effects 0.000 description 1
OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Natural products NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 1
229940104302 cytosine Drugs 0.000 description 1
NHVNXKFIZYSCEB-XLPZGREQSA-N dTTP Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)C1 NHVNXKFIZYSCEB-XLPZGREQSA-N 0.000 description 1
230000006378 damage Effects 0.000 description 1
230000007812 deficiency Effects 0.000 description 1
230000002939 deleterious effect Effects 0.000 description 1
229960003957 dexamethasone Drugs 0.000 description 1
UREBDLICKHMUKA-CXSFZGCWSA-N dexamethasone Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@]2(F)[C@@H]1[C@@H]1C[C@@H](C)[C@@](C(=O)CO)(O)[C@@]1(C)C[C@@H]2O UREBDLICKHMUKA-CXSFZGCWSA-N 0.000 description 1
108091007734 digestive enzymes Proteins 0.000 description 1
102000038379 digestive enzymes Human genes 0.000 description 1
239000000539 dimer Substances 0.000 description 1
150000002019 disulfides Chemical class 0.000 description 1
238000010828 elution Methods 0.000 description 1
230000002616 endonucleolytic effect Effects 0.000 description 1
238000006911 enzymatic reaction Methods 0.000 description 1
102000013165 exonuclease Human genes 0.000 description 1
238000000855 fermentation Methods 0.000 description 1
230000004151 fermentation Effects 0.000 description 1
238000005194 fractionation Methods 0.000 description 1
102000034356 gene-regulatory proteins Human genes 0.000 description 1
108091006104 gene-regulatory proteins Proteins 0.000 description 1
239000003862 glucocorticoid Substances 0.000 description 1
235000013922 glutamic acid Nutrition 0.000 description 1
239000004220 glutamic acid Substances 0.000 description 1
ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
108010042598 glutamyl-aspartyl-glycine Proteins 0.000 description 1
108010049041 glutamylalanine Proteins 0.000 description 1
108010000434 glycyl-alanyl-leucine Proteins 0.000 description 1
108010050848 glycylleucine Proteins 0.000 description 1
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
230000036541 health Effects 0.000 description 1
XLYOFNOQVPJJNP-ZSJDYOACSA-N heavy water Substances [2H]O[2H] XLYOFNOQVPJJNP-ZSJDYOACSA-N 0.000 description 1
HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
108010025306 histidylleucine Proteins 0.000 description 1
239000001257 hydrogen Substances 0.000 description 1
229910052739 hydrogen Inorganic materials 0.000 description 1
XMBWDFGMSWQBCA-UHFFFAOYSA-N hydrogen iodide Chemical compound I XMBWDFGMSWQBCA-UHFFFAOYSA-N 0.000 description 1
230000001771 impaired effect Effects 0.000 description 1
238000000338 in vitro Methods 0.000 description 1
230000002779 inactivation Effects 0.000 description 1
238000010348 incorporation Methods 0.000 description 1
238000001802 infusion Methods 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
230000005764 inhibitory process Effects 0.000 description 1
206010022498 insulinoma Diseases 0.000 description 1
230000003993 interaction Effects 0.000 description 1
150000002500 ions Chemical class 0.000 description 1
AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
229960000310 isoleucine Drugs 0.000 description 1
108010034529 leucyl-lysine Proteins 0.000 description 1
235000019421 lipase Nutrition 0.000 description 1
229910052744 lithium Inorganic materials 0.000 description 1
108010054155 lysyllysine Proteins 0.000 description 1
GMKMEZVLHJARHF-SYDPRGILSA-N meso-2,6-diaminopimelic acid Chemical compound [O-]C(=O)[C@@H]([NH3+])CCC[C@@H]([NH3+])C([O-])=O GMKMEZVLHJARHF-SYDPRGILSA-N 0.000 description 1
229930182817 methionine Natural products 0.000 description 1
230000002906 microbiologic effect Effects 0.000 description 1
238000006386 neutralization reaction Methods 0.000 description 1
102000039446 nucleic acids Human genes 0.000 description 1
108020004707 nucleic acids Proteins 0.000 description 1
150000007523 nucleic acids Chemical class 0.000 description 1
235000015097 nutrients Nutrition 0.000 description 1
210000003463 organelle Anatomy 0.000 description 1
238000010979 pH adjustment Methods 0.000 description 1
210000000277 pancreatic duct Anatomy 0.000 description 1
208000021255 pancreatic insulinoma Diseases 0.000 description 1
230000001575 pathological effect Effects 0.000 description 1
VLTRZXGMWDSKGL-UHFFFAOYSA-M perchlorate Inorganic materials [O-]Cl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-M 0.000 description 1
VLTRZXGMWDSKGL-UHFFFAOYSA-N perchloric acid Chemical compound OCl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-N 0.000 description 1
150000002989 phenols Chemical class 0.000 description 1
COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
108010012581 phenylalanylglutamate Proteins 0.000 description 1
108010051242 phenylalanylserine Proteins 0.000 description 1
150000003014 phosphoric acid esters Chemical class 0.000 description 1
208000010916 pituitary tumor Diseases 0.000 description 1
238000013492 plasmid preparation Methods 0.000 description 1
239000013600 plasmid vector Substances 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
108010057578 pregrowth hormone Proteins 0.000 description 1
238000004321 preservation Methods 0.000 description 1
238000012545 processing Methods 0.000 description 1
108010031719 prolyl-serine Proteins 0.000 description 1
108010090894 prolylleucine Proteins 0.000 description 1
BDERNNFJNOPAEC-UHFFFAOYSA-N propan-1-ol Chemical compound CCCO BDERNNFJNOPAEC-UHFFFAOYSA-N 0.000 description 1
238000011084 recovery Methods 0.000 description 1
230000009467 reduction Effects 0.000 description 1
230000029865 regulation of blood pressure Effects 0.000 description 1
230000001105 regulatory effect Effects 0.000 description 1
238000004153 renaturation Methods 0.000 description 1
230000003362 replicative effect Effects 0.000 description 1
239000002336 ribonucleotide Substances 0.000 description 1
125000002652 ribonucleotide group Chemical group 0.000 description 1
238000007363 ring formation reaction Methods 0.000 description 1
229920002477 rna polymer Polymers 0.000 description 1
238000012216 screening Methods 0.000 description 1
230000028327 secretion Effects 0.000 description 1
238000004062 sedimentation Methods 0.000 description 1
230000008684 selective degradation Effects 0.000 description 1
230000005783 single-strand break Effects 0.000 description 1
239000011780 sodium chloride Substances 0.000 description 1
239000007787 solid Substances 0.000 description 1
238000010561 standard procedure Methods 0.000 description 1
239000006228 supernatant Substances 0.000 description 1
238000001356 surgical procedure Methods 0.000 description 1
238000004114 suspension culture Methods 0.000 description 1
230000002195 synergetic effect Effects 0.000 description 1
229940037128 systemic glucocorticoids Drugs 0.000 description 1
230000001225 therapeutic effect Effects 0.000 description 1
150000003573 thiols Chemical class 0.000 description 1
239000005495 thyroid hormone Substances 0.000 description 1
229940036555 thyroid hormone Drugs 0.000 description 1
230000001131 transforming effect Effects 0.000 description 1
230000001052 transient effect Effects 0.000 description 1
UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 description 1
239000012137 tryptone Substances 0.000 description 1
108010080629 tryptophan-leucine Proteins 0.000 description 1
108010015666 tryptophyl-leucyl-glutamic acid Proteins 0.000 description 1
OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
229940035893 uracil Drugs 0.000 description 1
108700026220 vif Genes Proteins 0.000 description 1
238000005406 washing Methods 0.000 description 1
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
238000005303 weighing Methods 0.000 description 1
239000012138 yeast extract Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/10—Cells modified by introduction of foreign genetic material
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1096—Processes for the isolation, preparation or purification of DNA or RNA cDNA Synthesis; Subtracted cDNA library construction, e.g. RT, RT-PCR
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/57518—Placental lactogen; Chorionic somatomammotropin
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/62—Insulins
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Genetics & Genomics (AREA)
Organic Chemistry (AREA)
Engineering & Computer Science (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
Bioinformatics & Cheminformatics (AREA)
Biotechnology (AREA)
General Engineering & Computer Science (AREA)
Biomedical Technology (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
Molecular Biology (AREA)
Microbiology (AREA)
Biophysics (AREA)
Plant Pathology (AREA)
Physics & Mathematics (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Endocrinology (AREA)
Gastroenterology & Hepatology (AREA)
Toxicology (AREA)
Medicinal Chemistry (AREA)
Cell Biology (AREA)
Chemical Kinetics & Catalysis (AREA)
General Chemical & Material Sciences (AREA)
Bioinformatics & Computational Biology (AREA)
Pregnancy & Childbirth (AREA)
Diabetes (AREA)
Crystallography & Structural Chemistry (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Enzymes And Modification Thereof (AREA)

GB22417/78A 1977-05-27 1978-05-25 Recombinant dna transfer vector and microorganism containing a gene from a higher organism Expired GB1565190A (en)

Priority Applications (2)

Application Number	Priority Date	Filing Date	Title
GB7926492A GB2027610B (en)	1978-05-25	1979-07-30	Regeneration of ion exchange materials
MY1984121A MY8400121A (en)	1978-05-25	1984-12-31	Regeneration of ion exchange materials

Applications Claiming Priority (7)

Application Number	Priority Date	Filing Date	Title
US80134377A	1977-05-27	1977-05-27
US80502377A	1977-06-09	1977-06-09
US89770978A	1978-04-19	1978-04-19
US05897710 US4363877B1 (en)	1977-09-23	1978-04-19	Recombinant dna transfer vectors
US05/898,887 US4264731A (en)	1977-05-27	1978-04-21	DNA Joining method
US89900278A	1978-04-26	1978-04-26
US89900378A	1978-04-26	1978-04-26

Publications (1)

Publication Number	Publication Date
GB1565190A true GB1565190A (en)	1980-04-16

Family

ID=27569921

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
GB22417/78A Expired GB1565190A (en)	1977-05-27	1978-05-25	Recombinant dna transfer vector and microorganism containing a gene from a higher organism

Country Status (21)

Country	Link
JP (1)	JPH0659218B2 (sv)
AR (1)	AR225404A1 (sv)
AU (1)	AU521903B2 (sv)
BE (1)	BE867424A (sv)
BG (1)	BG40319A3 (sv)
CH (1)	CH642680A5 (sv)
DD (1)	DD145927A5 (sv)
DE (2)	DE2858357C2 (sv)
DK (2)	DK233278A (sv)
FI (1)	FI64640C (sv)
FR (1)	FR2392033B1 (sv)
GB (1)	GB1565190A (sv)
GR (1)	GR73552B (sv)
IL (1)	IL54790A (sv)
IT (1)	IT1094934B (sv)
LU (1)	LU79714A1 (sv)
NL (1)	NL7805591A (sv)
NZ (1)	NZ187300A (sv)
PL (1)	PL140200B1 (sv)
PT (1)	PT68082B (sv)
SE (4)	SE451461B (sv)

Cited By (12)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP0035781A2 (en) *	1980-03-10	1981-09-16	The Regents Of The University Of California	Microbiological syntheses of beta endorphin
EP0037687A2 (en) *	1980-04-03	1981-10-14	Abbott Laboratories	Recombinant deoxyribonucleid acid which codes for plasminogen activator and method of making plasminogen activator protein therefrom
EP0054330A2 (en) *	1980-12-12	1982-06-23	Unilever N.V.	DNA sequences encoding various allelic forms of mature thaumatin, recombinant plasmids comprising said DNA's and a process for their preparation, bacterial cultures comprising said recombinant plasmids, and method for producing mature thaumatin
EP0054331A1 (en) *	1980-12-12	1982-06-23	Unilever N.V.	Structural genes encoding the various allelic and maturation forms of preprothaumatin and mutations thereof, recombinant cloning vehicles comprising said structural genes and expression thereof in transformed microbial host cells
US4338397A (en)	1980-04-11	1982-07-06	President And Fellows Of Harvard College	Mature protein synthesis
US4469791A (en) *	1980-02-15	1984-09-04	Cpc International Inc.	Genetically engineered microorganisms for massive production of amylolytic enzymes and process for preparing same
US4693973A (en) *	1982-08-17	1987-09-15	Biogen N.V.	DNA sequences, recombinant DNA molecules and processes for producing bovine growth hormone-like polypeptides in high yield
US4695543A (en) *	1982-03-23	1987-09-22	Bristol-Myers Company	Alpha Interferon GX-1
US4748233A (en) *	1982-03-23	1988-05-31	Bristol-Myers Company	Alpha-interferon Gx-1
US5411951A (en) *	1984-10-04	1995-05-02	Monsanto Company	Prolonged release of biologically active somatotropin
US5474980A (en) *	1984-10-04	1995-12-12	Monsanto Company	Prolonged release of biologically active somatotropins
US6268122B1 (en)	1978-12-22	2001-07-31	Biogen, Inc.	Recombinant DNA molecules and their method of production

Families Citing this family (13)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
ZA782933B (en) *	1977-09-23	1979-05-30	Univ California	Purification of nucleotide sequences suitable for expression in bacteria
BR7807290A (pt) *	1977-11-08	1979-06-12	Genentech Inc	Plasmideo,processo para producao de um polipeptido especifico veiculo clonal,cultura bacteriana transformante,processo para produzir uma substancia imunogenica processo para preparar um gene estrutural,e polidesoxirribonucleotido de faixa dupla
GR71912B (sv) *	1978-08-11	1983-08-16	Univ California
JPS55150883A (en) *	1979-05-11	1980-11-25	Nakano Vinegar Co Ltd	Method of storing "mozuku"
ZA802992B (en) *	1979-06-01	1981-10-28	Univ California	Human pre-growth hormone
FR2458584A1 (fr) *	1979-06-08	1981-01-02	Pasteur Institut	Vecteurs pour le transfert et l'expression de materiel genetique dans une cellule eucaryote et procede pour la production d'une proteine determinee dans des cellules eucaryotes
US4342832A (en) *	1979-07-05	1982-08-03	Genentech, Inc.	Method of constructing a replicable cloning vehicle having quasi-synthetic genes
GR70279B (sv) *	1979-09-12	1982-09-03	Univ California
IL58765A (en) *	1979-11-21	1986-09-30	Yeda Res & Dev	Process for the production of essentially pure messenger rna of human fibroblast interferon and process for the production of interferon beta
DE3001928A1 (de) *	1980-01-19	1981-08-06	Hoechst Ag, 6000 Frankfurt	Genprodukt eines hoeheren organismus aus einem dieses gen enthaltenden mikroorganismus
CA1202581A (en) *	1980-03-27	1986-04-01	Saran A. Narang	Adaptor molecules for dna and their application to synthesis of gene-derived products
DK257988D0 (da) *	1988-05-11	1988-05-11	Novo Industri As	Nye peptider
DE4034702A1 (de) *	1990-10-31	1992-05-07	Siemens Ag	Verfahren und vorrichtung zur pruefung der aktiven werkzeuge von gesenkbiegemaschinen, insbesondere von biegestempeln

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB1521032A (en) *	1974-08-08	1978-08-09	Ici Ltd	Biological treatment

1978
- 1978-05-17 NZ NZ187300A patent/NZ187300A/xx unknown
- 1978-05-23 GR GR56309A patent/GR73552B/el unknown
- 1978-05-23 NL NL7805591A patent/NL7805591A/ not_active Application Discontinuation
- 1978-05-23 AR AR272286A patent/AR225404A1/es active
- 1978-05-24 PT PT68082A patent/PT68082B/pt unknown
- 1978-05-24 DE DE2858357A patent/DE2858357C2/de not_active Expired - Lifetime
- 1978-05-24 BE BE187995A patent/BE867424A/xx not_active IP Right Cessation
- 1978-05-24 DE DE19782822568 patent/DE2822568A1/de active Granted
- 1978-05-25 DD DD78205588A patent/DD145927A5/de unknown
- 1978-05-25 FR FR7815596A patent/FR2392033B1/fr not_active Expired
- 1978-05-25 GB GB22417/78A patent/GB1565190A/en not_active Expired
- 1978-05-25 AU AU36488/78A patent/AU521903B2/en not_active Expired
- 1978-05-26 SE SE7806086A patent/SE451461B/sv unknown
- 1978-05-26 CH CH581078A patent/CH642680A5/de not_active IP Right Cessation
- 1978-05-26 IL IL54790A patent/IL54790A/xx unknown
- 1978-05-26 FI FI781675A patent/FI64640C/fi not_active IP Right Cessation
- 1978-05-26 DK DK782332A patent/DK233278A/da not_active Application Discontinuation
- 1978-05-26 LU LU79714A patent/LU79714A1/xx unknown
- 1978-05-27 BG BG039878A patent/BG40319A3/xx unknown
- 1978-05-27 PL PL1978207176A patent/PL140200B1/pl unknown
- 1978-05-27 JP JP53063756A patent/JPH0659218B2/ja not_active Expired - Lifetime
- 1978-05-29 IT IT23930/78A patent/IT1094934B/it active
1983
- 1983-09-29 SE SE8305327A patent/SE8305327L/sv not_active Application Discontinuation
- 1983-09-29 SE SE8305329A patent/SE455794B/sv not_active Application Discontinuation
- 1983-09-29 SE SE8305328A patent/SE8305328D0/sv not_active Application Discontinuation
1991
- 1991-01-04 DK DK000791A patent/DK791A/da not_active Application Discontinuation

Cited By (21)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US6270955B1 (en)	1978-12-22	2001-08-07	Biogen, Inc.	Pharmaceutical compositions and methods for producing antibodies to hepatitis b virus and kits and methods for detecting antibodies to hepatitis b virus
US6268122B1 (en)	1978-12-22	2001-07-31	Biogen, Inc.	Recombinant DNA molecules and their method of production
US6297355B1 (en)	1978-12-22	2001-10-02	Biogen, Inc.	Polypeptides displaying HBV antigenicity or hbv antigen specificity
US4469791A (en) *	1980-02-15	1984-09-04	Cpc International Inc.	Genetically engineered microorganisms for massive production of amylolytic enzymes and process for preparing same
EP0035781A3 (en) *	1980-03-10	1982-02-10	The Regents Of The University Of California	Microbiological syntheses of beta endorphin
EP0035781A2 (en) *	1980-03-10	1981-09-16	The Regents Of The University Of California	Microbiological syntheses of beta endorphin
EP0037687A3 (en) *	1980-04-03	1982-02-17	Abbott Laboratories	Recombinant deoxyribonucleid acid which codes for plasminogen activator and method of making plasminogen activator protein therefrom
EP0037687A2 (en) *	1980-04-03	1981-10-14	Abbott Laboratories	Recombinant deoxyribonucleid acid which codes for plasminogen activator and method of making plasminogen activator protein therefrom
US4338397A (en)	1980-04-11	1982-07-06	President And Fellows Of Harvard College	Mature protein synthesis
EP0054330A3 (en) *	1980-12-12	1982-09-22	Unilever Nv	Dna sequences encoding the various allelic forms of mature thaumatin, and cloning vehicles comprising said dna's and their use in transforming microorganisms
EP0054331A1 (en) *	1980-12-12	1982-06-23	Unilever N.V.	Structural genes encoding the various allelic and maturation forms of preprothaumatin and mutations thereof, recombinant cloning vehicles comprising said structural genes and expression thereof in transformed microbial host cells
EP0054330A2 (en) *	1980-12-12	1982-06-23	Unilever N.V.	DNA sequences encoding various allelic forms of mature thaumatin, recombinant plasmids comprising said DNA's and a process for their preparation, bacterial cultures comprising said recombinant plasmids, and method for producing mature thaumatin
US4771000A (en) *	1980-12-12	1988-09-13	Internationale Octrooi Maatschappij Octropa B.V.	Structural genes encoding the various allelic and maturation forms of preprothaumatin, recombinant cloning vehicles comprising said structural genes and expression thereof in transformed microbial host cells
US4891316A (en) *	1980-12-12	1990-01-02	Unilever Patent Holdings B.V.	DNA sequences encoding the various allelic forms of mature thaumatin, and cloning vehicles, etc.
US4966842A (en) *	1980-12-12	1990-10-30	Unilever Patent Holdings B.V.	Structural genes encoding the various allelic and maturation forms of preprothaumatin recombinant cloning vehicles, comprising said structural genes and expression thereof in transformed microbial host cells
US4695543A (en) *	1982-03-23	1987-09-22	Bristol-Myers Company	Alpha Interferon GX-1
US4748233A (en) *	1982-03-23	1988-05-31	Bristol-Myers Company	Alpha-interferon Gx-1
US4693973A (en) *	1982-08-17	1987-09-15	Biogen N.V.	DNA sequences, recombinant DNA molecules and processes for producing bovine growth hormone-like polypeptides in high yield
US5474980A (en) *	1984-10-04	1995-12-12	Monsanto Company	Prolonged release of biologically active somatotropins
US5595971A (en) *	1984-10-04	1997-01-21	Monsanto Company	Prolonged release of biologically active polypeptides
US5411951A (en) *	1984-10-04	1995-05-02	Monsanto Company	Prolonged release of biologically active somatotropin

Also Published As

Publication number	Publication date
SE8305327D0 (sv)	1983-09-29
BE867424A (fr)	1978-09-18
SE8305328L (sv)	1983-09-29
FI781675A (fi)	1978-11-28
PT68082A (en)	1978-06-01
IL54790A (en)	1983-07-31
DK233278A (da)	1978-11-28
DK791D0 (da)	1991-01-04
JPS5449387A (en)	1979-04-18
FR2392033A1 (fr)	1978-12-22
SE8305329L (sv)	1983-09-29
BG40319A3 (en)	1986-11-14
AU521903B2 (en)	1982-05-06
GR73552B (sv)	1984-03-14
IT1094934B (it)	1985-08-10
DE2858357C2 (sv)	1990-03-15
PL207176A1 (pl)	1979-03-26
FI64640B (fi)	1983-08-31
DE2822568C2 (sv)	1989-08-31
PT68082B (en)	1980-02-20
FI64640C (fi)	1983-12-12
DD145927A5 (de)	1981-01-14
NZ187300A (en)	1982-08-17
SE8305327L (sv)	1983-09-29
SE455794B (sv)	1988-08-08
DE2822568A1 (de)	1978-12-14
IT7823930A0 (it)	1978-05-29
IL54790A0 (en)	1978-07-31
SE8305329D0 (sv)	1983-09-29
SE7806086L (sv)	1978-11-28
AU3648878A (en)	1979-11-29
DK791A (da)	1991-01-04
FR2392033B1 (fr)	1985-09-13
SE451461B (sv)	1987-10-12
LU79714A1 (fr)	1978-11-06
SE8305328D0 (sv)	1983-09-29
NL7805591A (nl)	1978-11-29
AR225404A1 (es)	1982-03-31
JPH0659218B2 (ja)	1994-08-10
PL140200B1 (en)	1987-04-30
CH642680A5 (en)	1984-04-30

Publication	Publication Date	Title
GB1565190A (en)	1980-04-16	Recombinant dna transfer vector and microorganism containing a gene from a higher organism
US4440859A (en)	1984-04-03	Method for producing recombinant bacterial plasmids containing the coding sequences of higher organisms
US4652525A (en)	1987-03-24	Recombinant bacterial plasmids containing the coding sequences of insulin genes
KR870000701B1 (ko)	1987-04-07	인체 성장 호르몬의 제조방법
EP0020147B2 (en)	1988-01-13	A dna transfer vector for human pre-growth hormone, a microorganism transformed thereby, and a method of cloning therefor
KR860001230B1 (ko)	1986-08-30	이중 가닥 dna의 분할 방법
US4431740A (en)	1984-02-14	DNA Transfer vector and transformed microorganism containing human proinsulin and pre-proinsulin genes
JP2637393B2 (ja)	1997-08-06	プロインシュリンおよびプレプロインシュリン産生暗号を有するヒト遺伝子
EP0067026A1 (en)	1982-12-15	Process for cloning bovine hormone gene, and plasmids and plasmid hosts for use therein
CA1156166A (en)	1983-11-01	Recombinant bacterial plasmids containing the coding sequences of insulin genes
IE47274B1 (en)	1984-02-08	Recombinant dna transfer vector and micro-organism containing a gene from a higher organism
KR840001441B1 (ko)	1984-09-27	고등생물의 특정 단백질에 대한 뉴클레오티드 배열을 함유하는 dna전달 매개체의 제조방법
FI75185C (sv)	1988-05-09	DNA-överföringsvektor, vilken innehåller en för insulin kodande nukleo tidsekvens.
FI65447C (fi)	1984-05-10	Foerfarande foer framstaellning av en bakterie som innehaolleren foer tillvaexthormon kodande nukleotidsekvens
FI74732B (fi)	1987-11-30	Dna-oeverfoeringsvektor, vilken innehaoller en nukleotidsekvens som kodar foer tillvaexthormon.
FI65446C (fi)	1984-05-10	Foerfarande foer framstaellning av en bakterie som innehaolleren foer insulin kodande nukleotidsekvens
CS227002B2 (cs)	1984-04-16	Způsob výroby vektoru pro přenos DNA
AT386607B (de)	1988-09-26	Verfahren zum herstellen eines dns-transfer-vektors
CS227013B2 (cs)	1984-04-16	Způsob výroby vektoru pro přenos DNA
AT386609B (de)	1988-09-26	Verfahren zum herstellen eines mikroorganismus
CA1302321C (en)	1992-06-02	Preparation of polypeptides
HU193866B (en)	1987-12-28	Process for preparing plasmid and e.coli bakterium comprising dna sequence and coding humane growth hormone
CS227033B2 (cs)	1984-04-16	Způsob pěstování mikroorganismu s obsahem a replikací vektoru pro přenos DNA
AT386608B (de)	1988-09-26	Verfahren zum herstellen eines mikroorganismus
SU1205777A3 (ru)	1986-01-15	Способ получени вектора,имеющего нуклеотидную последовательность,кодирующую протеин

Legal Events

Date	Code	Title	Description
1980-07-02	PS	Patent sealed [section 19, patents act 1949]
1998-06-17	PE20	Patent expired after termination of 20 years	Effective date: 19980524