BG62492B1 - Състави и методи за идентифициране и синтез насиалилтрансферази - Google Patents

Състави и методи за идентифициране и синтез насиалилтрансферази Download PDF

Info

Publication number: BG62492B1
Authority: BG; Bulgaria
Prior art keywords: sialyltransferase; val; sequence; dna; gly
Prior art date: 1992-03-09
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 - Lifetime

Application number

BG99100A

Other languages

Bulgarian (bg)

English (en)

Other versions

BG99100A (bg

Inventor

James E. Paulson

Xiaohong Wen

Brian D. Livingston

William Gillespie

Sorge Kelm

Alma L. Burlingame

Katalin Medzihradszky

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.)

Regents of the University of California, San Diego

Cytel Corp

Original Assignee

Regents of the University of California, San Diego

Cytel Corp

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.)

1992-03-09

Filing date

1994-10-07

Publication date

1999-12-30

1994-10-07 Application filed by Regents of the University of California, San Diego, Cytel Corp filed Critical Regents of the University of California, San Diego

1995-05-31 Publication of BG99100A publication Critical patent/BG99100A/bg

1999-12-30 Publication of BG62492B1 publication Critical patent/BG62492B1/bg

2014-10-07 Anticipated expiration legal-status Critical

Status Expired - Lifetime legal-status Critical Current

Links

108090000141 Sialyltransferases Proteins 0.000 title claims description 297
102000003838 Sialyltransferases Human genes 0.000 title claims description 282
239000000203 mixture Substances 0.000 title claims description 19
238000000034 method Methods 0.000 title abstract description 61
230000015572 biosynthetic process Effects 0.000 title description 10
238000003786 synthesis reaction Methods 0.000 title description 10
108020004414 DNA Proteins 0.000 claims abstract description 62
108090000765 processed proteins & peptides Proteins 0.000 claims description 69
150000001413 amino acids Chemical class 0.000 claims description 62
102000053602 DNA Human genes 0.000 claims description 56
125000003275 alpha amino acid group Chemical group 0.000 claims description 51
102000004190 Enzymes Human genes 0.000 claims description 46
108090000790 Enzymes Proteins 0.000 claims description 46
102000004196 processed proteins & peptides Human genes 0.000 claims description 46
230000000694 effects Effects 0.000 claims description 37
229920001184 polypeptide Polymers 0.000 claims description 29
230000003197 catalytic effect Effects 0.000 claims description 19
239000013604 expression vector Substances 0.000 claims description 18
230000001086 cytosolic effect Effects 0.000 claims description 12
238000001727 in vivo Methods 0.000 claims description 9
238000003259 recombinant expression Methods 0.000 claims description 9
108010005774 beta-Galactosidase Proteins 0.000 claims description 3
239000000126 substance Substances 0.000 claims description 3
230000001747 exhibiting effect Effects 0.000 claims description 2
102000005936 beta-Galactosidase Human genes 0.000 claims 1
230000000717 retained effect Effects 0.000 claims 1
238000004519 manufacturing process Methods 0.000 abstract description 11
238000002360 preparation method Methods 0.000 abstract description 7
210000004027 cell Anatomy 0.000 description 110
108090000623 proteins and genes Proteins 0.000 description 108
239000012634 fragment Substances 0.000 description 67
239000002299 complementary DNA Substances 0.000 description 65
235000001014 amino acid Nutrition 0.000 description 63
229940024606 amino acid Drugs 0.000 description 61
235000018102 proteins Nutrition 0.000 description 61
102000004169 proteins and genes Human genes 0.000 description 61
241000700159 Rattus Species 0.000 description 42
230000014509 gene expression Effects 0.000 description 40
102000040430 polynucleotide Human genes 0.000 description 37
108091033319 polynucleotide Proteins 0.000 description 37
239000002157 polynucleotide Substances 0.000 description 37
238000003752 polymerase chain reaction Methods 0.000 description 35
239000002609 medium Substances 0.000 description 33
239000013615 primer Substances 0.000 description 32
108091034117 Oligonucleotide Proteins 0.000 description 26
239000013598 vector Substances 0.000 description 26
239000012528 membrane Substances 0.000 description 23
238000009396 hybridization Methods 0.000 description 22
239000002773 nucleotide Substances 0.000 description 22
125000003729 nucleotide group Chemical group 0.000 description 22
239000013612 plasmid Substances 0.000 description 22
239000000523 sample Substances 0.000 description 22
239000000370 acceptor Substances 0.000 description 21
108020004999 messenger RNA Proteins 0.000 description 21
210000001519 tissue Anatomy 0.000 description 21
210000004185 liver Anatomy 0.000 description 19
SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 description 18
238000012217 deletion Methods 0.000 description 18
230000037430 deletion Effects 0.000 description 18
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical group 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 description 18
108700026244 Open Reading Frames Proteins 0.000 description 17
239000000872 buffer Substances 0.000 description 17
150000002500 ions Chemical class 0.000 description 17
238000006467 substitution reaction Methods 0.000 description 17
108091032973 (ribonucleotides)n+m Proteins 0.000 description 16
108700023372 Glycosyltransferases Proteins 0.000 description 16
108010076504 Protein Sorting Signals Proteins 0.000 description 16
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 16
238000002474 experimental method Methods 0.000 description 16
241000894007 species Species 0.000 description 16
238000013518 transcription Methods 0.000 description 16
230000035897 transcription Effects 0.000 description 16
102100029231 Alpha-2,8-sialyltransferase 8B Human genes 0.000 description 15
101710105328 Alpha-2,8-sialyltransferase 8B Proteins 0.000 description 15
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 15
241000700605 Viruses Species 0.000 description 15
238000004458 analytical method Methods 0.000 description 15
229920001542 oligosaccharide Polymers 0.000 description 15
150000002482 oligosaccharides Chemical class 0.000 description 15
239000000047 product Substances 0.000 description 15
238000003199 nucleic acid amplification method Methods 0.000 description 14
SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 description 14
101100007328 Cocos nucifera COS-1 gene Proteins 0.000 description 13
240000004808 Saccharomyces cerevisiae Species 0.000 description 13
235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 13
230000003321 amplification Effects 0.000 description 13
102000045442 glycosyltransferase activity proteins Human genes 0.000 description 13
108700014210 glycosyltransferase activity proteins Proteins 0.000 description 13
241000282414 Homo sapiens Species 0.000 description 12
108091028043 Nucleic acid sequence Proteins 0.000 description 12
210000004556 brain Anatomy 0.000 description 12
238000006243 chemical reaction Methods 0.000 description 12
108020001507 fusion proteins Proteins 0.000 description 12
102000037865 fusion proteins Human genes 0.000 description 12
241001465754 Metazoa Species 0.000 description 11
108090000631 Trypsin Proteins 0.000 description 11
102000004142 Trypsin Human genes 0.000 description 11
238000010367 cloning Methods 0.000 description 11
230000000295 complement effect Effects 0.000 description 11
239000000758 substrate Substances 0.000 description 11
239000012588 trypsin Substances 0.000 description 11
OVRNDRQMDRJTHS-RTRLPJTCSA-N N-acetyl-D-glucosamine Chemical compound CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-RTRLPJTCSA-N 0.000 description 10
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
125000000539 amino acid group Chemical group 0.000 description 10
230000004927 fusion Effects 0.000 description 10
150000007523 nucleic acids Chemical class 0.000 description 10
238000012163 sequencing technique Methods 0.000 description 10
125000005629 sialic acid group Chemical group 0.000 description 10
238000001890 transfection Methods 0.000 description 10
102000004877 Insulin Human genes 0.000 description 9
108090001061 Insulin Proteins 0.000 description 9
OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 description 9
MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 description 9
239000002253 acid Substances 0.000 description 9
238000001360 collision-induced dissociation Methods 0.000 description 9
239000003599 detergent Substances 0.000 description 9
230000002255 enzymatic effect Effects 0.000 description 9
230000002209 hydrophobic effect Effects 0.000 description 9
238000003780 insertion Methods 0.000 description 9
230000037431 insertion Effects 0.000 description 9
229940125396 insulin Drugs 0.000 description 9
238000010369 molecular cloning Methods 0.000 description 9
238000000746 purification Methods 0.000 description 9
238000013519 translation Methods 0.000 description 9
101800000246 Allatostatin-1 Proteins 0.000 description 8
102100036608 Aspartate aminotransferase, cytoplasmic Human genes 0.000 description 8
OBMZMSLWNNWEJA-XNCRXQDQSA-N C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 Chemical compound C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 OBMZMSLWNNWEJA-XNCRXQDQSA-N 0.000 description 8
101710176384 Peptide 1 Proteins 0.000 description 8
108010022394 Threonine synthase Proteins 0.000 description 8
238000003556 assay Methods 0.000 description 8
102000004419 dihydrofolate reductase Human genes 0.000 description 8
238000011534 incubation Methods 0.000 description 8
102000039446 nucleic acids Human genes 0.000 description 8
108020004707 nucleic acids Proteins 0.000 description 8
230000010076 replication Effects 0.000 description 8
108091008146 restriction endonucleases Proteins 0.000 description 8
238000012546 transfer Methods 0.000 description 8
230000009261 transgenic effect Effects 0.000 description 8
108010053481 Antifreeze Proteins Proteins 0.000 description 7
101500011070 Diploptera punctata Allatostatin-2 Proteins 0.000 description 7
241000588724 Escherichia coli Species 0.000 description 7
229930186217 Glycolipid Natural products 0.000 description 7
238000007792 addition Methods 0.000 description 7
150000001720 carbohydrates Chemical group 0.000 description 7
238000011161 development Methods 0.000 description 7
230000018109 developmental process Effects 0.000 description 7
230000029087 digestion Effects 0.000 description 7
239000003623 enhancer Substances 0.000 description 7
239000013613 expression plasmid Substances 0.000 description 7
238000013467 fragmentation Methods 0.000 description 7
238000006062 fragmentation reaction Methods 0.000 description 7
230000006870 function Effects 0.000 description 7
210000003079 salivary gland Anatomy 0.000 description 7
241000701447 unidentified baculovirus Species 0.000 description 7
108020004705 Codon Proteins 0.000 description 6
108020004511 Recombinant DNA Proteins 0.000 description 6
108010091769 Shiga Toxin 1 Proteins 0.000 description 6
241000282887 Suidae Species 0.000 description 6
102100029932 Syntaxin-1A Human genes 0.000 description 6
238000013459 approach Methods 0.000 description 6
238000004113 cell culture Methods 0.000 description 6
230000001413 cellular effect Effects 0.000 description 6
238000012512 characterization method Methods 0.000 description 6
235000021186 dishes Nutrition 0.000 description 6
230000012010 growth Effects 0.000 description 6
238000000338 in vitro Methods 0.000 description 6
239000003446 ligand Substances 0.000 description 6
238000004949 mass spectrometry Methods 0.000 description 6
238000002703 mutagenesis Methods 0.000 description 6
231100000350 mutagenesis Toxicity 0.000 description 6
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 6
241000283690 Bos taurus Species 0.000 description 5
101710136075 CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase Proteins 0.000 description 5
102100029962 CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase Human genes 0.000 description 5
108020004635 Complementary DNA Proteins 0.000 description 5
102000003886 Glycoproteins Human genes 0.000 description 5
108090000288 Glycoproteins Proteins 0.000 description 5
FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 5
238000012300 Sequence Analysis Methods 0.000 description 5
108091036066 Three prime untranslated region Proteins 0.000 description 5
108020004566 Transfer RNA Proteins 0.000 description 5
108700019146 Transgenes Proteins 0.000 description 5
HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 5
210000004899 c-terminal region Anatomy 0.000 description 5
125000000837 carbohydrate group Chemical group 0.000 description 5
150000001875 compounds Chemical class 0.000 description 5
-1 e.g. Chemical group 0.000 description 5
238000010828 elution Methods 0.000 description 5
238000004992 fast atom bombardment mass spectroscopy Methods 0.000 description 5
239000000499 gel Substances 0.000 description 5
239000011159 matrix material Substances 0.000 description 5
229960000485 methotrexate Drugs 0.000 description 5
230000035772 mutation Effects 0.000 description 5
210000002966 serum Anatomy 0.000 description 5
239000011780 sodium chloride Substances 0.000 description 5
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
235000000346 sugar Nutrition 0.000 description 5
230000009466 transformation Effects 0.000 description 5
230000003612 virological effect Effects 0.000 description 5
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
229920000936 Agarose Polymers 0.000 description 4
108700028369 Alleles Proteins 0.000 description 4
XKRFYHLGVUSROY-UHFFFAOYSA-N Argon Chemical compound [Ar] XKRFYHLGVUSROY-UHFFFAOYSA-N 0.000 description 4
108060003306 Galactosyltransferase Proteins 0.000 description 4
XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 4
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
239000000020 Nitrocellulose Substances 0.000 description 4
229920002684 Sepharose Polymers 0.000 description 4
150000007513 acids Chemical class 0.000 description 4
238000001042 affinity chromatography Methods 0.000 description 4
230000001580 bacterial effect Effects 0.000 description 4
230000008901 benefit Effects 0.000 description 4
210000004369 blood Anatomy 0.000 description 4
239000008280 blood Substances 0.000 description 4
229910052799 carbon Inorganic materials 0.000 description 4
238000010276 construction Methods 0.000 description 4
229940079593 drug Drugs 0.000 description 4
239000003814 drug Substances 0.000 description 4
150000002270 gangliosides Chemical class 0.000 description 4
210000002288 golgi apparatus Anatomy 0.000 description 4
238000000227 grinding Methods 0.000 description 4
239000001963 growth medium Substances 0.000 description 4
238000002744 homologous recombination Methods 0.000 description 4
230000006801 homologous recombination Effects 0.000 description 4
238000010348 incorporation Methods 0.000 description 4
238000002955 isolation Methods 0.000 description 4
210000003292 kidney cell Anatomy 0.000 description 4
239000003550 marker Substances 0.000 description 4
229920001220 nitrocellulos Polymers 0.000 description 4
229920002401 polyacrylamide Polymers 0.000 description 4
230000008569 process Effects 0.000 description 4
239000002904 solvent Substances 0.000 description 4
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
102000002260 Alkaline Phosphatase Human genes 0.000 description 3
108020004774 Alkaline Phosphatase Proteins 0.000 description 3
241000894006 Bacteria Species 0.000 description 3
108091026890 Coding region Proteins 0.000 description 3
208000033962 Fontaine progeroid syndrome Diseases 0.000 description 3
102000030902 Galactosyltransferase Human genes 0.000 description 3
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
102000051366 Glycosyltransferases Human genes 0.000 description 3
AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 3
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 3
GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 3
229930193140 Neomycin Natural products 0.000 description 3
102100023472 P-selectin Human genes 0.000 description 3
229910019142 PO4 Inorganic materials 0.000 description 3
108091000080 Phosphotransferase Proteins 0.000 description 3
239000007983 Tris buffer Substances 0.000 description 3
QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 3
239000011543 agarose gel Substances 0.000 description 3
125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 3
244000309466 calf Species 0.000 description 3
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
230000015556 catabolic process Effects 0.000 description 3
108020001778 catalytic domains Proteins 0.000 description 3
210000000170 cell membrane Anatomy 0.000 description 3
150000001793 charged compounds Chemical class 0.000 description 3
239000003153 chemical reaction reagent Substances 0.000 description 3
238000001514 detection method Methods 0.000 description 3
238000000502 dialysis Methods 0.000 description 3
230000004069 differentiation Effects 0.000 description 3
238000002290 gas chromatography-mass spectrometry Methods 0.000 description 3
239000012535 impurity Substances 0.000 description 3
210000003734 kidney Anatomy 0.000 description 3
239000008101 lactose Substances 0.000 description 3
125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 3
239000000463 material Substances 0.000 description 3
230000004048 modification Effects 0.000 description 3
238000012986 modification Methods 0.000 description 3
229960004927 neomycin Drugs 0.000 description 3
229940060155 neuac Drugs 0.000 description 3
235000015097 nutrients Nutrition 0.000 description 3
230000037361 pathway Effects 0.000 description 3
102000020233 phosphotransferase Human genes 0.000 description 3
230000002797 proteolythic effect Effects 0.000 description 3
230000003248 secreting effect Effects 0.000 description 3
230000011664 signaling Effects 0.000 description 3
239000000243 solution Substances 0.000 description 3
238000001228 spectrum Methods 0.000 description 3
239000006228 supernatant Substances 0.000 description 3
210000004876 tela submucosa Anatomy 0.000 description 3
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 2
GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 description 2
HVCOBJNICQPDBP-UHFFFAOYSA-N 3-[3-[3,5-dihydroxy-6-methyl-4-(3,4,5-trihydroxy-6-methyloxan-2-yl)oxyoxan-2-yl]oxydecanoyloxy]decanoic acid;hydrate Chemical compound O.OC1C(OC(CC(=O)OC(CCCCCCC)CC(O)=O)CCCCCCC)OC(C)C(O)C1OC1C(O)C(O)C(O)C(C)O1 HVCOBJNICQPDBP-UHFFFAOYSA-N 0.000 description 2
101710144734 48 kDa protein Proteins 0.000 description 2
102000013563 Acid Phosphatase Human genes 0.000 description 2
108010051457 Acid Phosphatase Proteins 0.000 description 2
101001057129 Bacillus cereus Enterotoxin Proteins 0.000 description 2
101710083568 CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 Proteins 0.000 description 2
102100027098 CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 Human genes 0.000 description 2
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 2
OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
241000282693 Cercopithecidae Species 0.000 description 2
HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
241000701022 Cytomegalovirus Species 0.000 description 2
239000003155 DNA primer Substances 0.000 description 2
239000006144 Dulbecco’s modiﬁed Eagle's medium Substances 0.000 description 2
241001646716 Escherichia coli K-12 Species 0.000 description 2
241000206602 Eukaryota Species 0.000 description 2
ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
108010019236 Fucosyltransferases Proteins 0.000 description 2
241000238631 Hexapoda Species 0.000 description 2
FDGQSTZJBFJUBT-UHFFFAOYSA-N Hypoxanthine Natural products O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
108091026898 Leader sequence (mRNA) Proteins 0.000 description 2
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
241001529936 Murinae Species 0.000 description 2
101000700655 Mycobacterium leprae (strain TN) Serine-rich antigen Proteins 0.000 description 2
102000007524 N-Acetylgalactosaminyltransferases Human genes 0.000 description 2
108010046220 N-Acetylgalactosaminyltransferases Proteins 0.000 description 2
SQVRNKJHWKZAKO-LUWBGTNYSA-N N-acetylneuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)CC(O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-LUWBGTNYSA-N 0.000 description 2
108010069196 Neural Cell Adhesion Molecules Proteins 0.000 description 2
102100023616 Neural cell adhesion molecule L1-like protein Human genes 0.000 description 2
102400001270 Neuronostatin Human genes 0.000 description 2
238000000636 Northern blotting Methods 0.000 description 2
108020005187 Oligonucleotide Probes Proteins 0.000 description 2
108010035766 P-Selectin Proteins 0.000 description 2
239000002033 PVDF binder Substances 0.000 description 2
241000282322 Panthera Species 0.000 description 2
208000000474 Poliomyelitis Diseases 0.000 description 2
101710117586 S-arrestin Proteins 0.000 description 2
108010079723 Shiga Toxin Proteins 0.000 description 2
108091081024 Start codon Proteins 0.000 description 2
101150003725 TK gene Proteins 0.000 description 2
239000004098 Tetracycline Substances 0.000 description 2
IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
102000004357 Transferases Human genes 0.000 description 2
108090000992 Transferases Proteins 0.000 description 2
229920004890 Triton X-100 Polymers 0.000 description 2
239000013504 Triton X-100 Substances 0.000 description 2
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
239000000853 adhesive Substances 0.000 description 2
230000001070 adhesive effect Effects 0.000 description 2
229960000723 ampicillin Drugs 0.000 description 2
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 2
230000003698 anagen phase Effects 0.000 description 2
125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 2
229910052786 argon Inorganic materials 0.000 description 2
210000000270 basal cell Anatomy 0.000 description 2
239000011324 bead Substances 0.000 description 2
108010064886 beta-D-galactoside alpha 2-6-sialyltransferase Proteins 0.000 description 2
230000004071 biological effect Effects 0.000 description 2
210000001124 body fluid Anatomy 0.000 description 2
239000010839 body fluid Substances 0.000 description 2
RSKPLCGMBWEANE-UHFFFAOYSA-N cacodyl Chemical group C[As](C)[As](C)C RSKPLCGMBWEANE-UHFFFAOYSA-N 0.000 description 2
239000001110 calcium chloride Substances 0.000 description 2
229910001628 calcium chloride Inorganic materials 0.000 description 2
235000011148 calcium chloride Nutrition 0.000 description 2
235000014633 carbohydrates Nutrition 0.000 description 2
230000021164 cell adhesion Effects 0.000 description 2
238000003776 cleavage reaction Methods 0.000 description 2
210000003022 colostrum Anatomy 0.000 description 2
235000021277 colostrum Nutrition 0.000 description 2
230000001276 controlling effect Effects 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
230000030609 dephosphorylation Effects 0.000 description 2
238000006209 dephosphorylation reaction Methods 0.000 description 2
238000009826 distribution Methods 0.000 description 2
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 2
238000005516 engineering process Methods 0.000 description 2
210000003527 eukaryotic cell Anatomy 0.000 description 2
239000000284 extract Substances 0.000 description 2
238000000605 extraction Methods 0.000 description 2
230000001605 fetal effect Effects 0.000 description 2
238000010230 functional analysis Methods 0.000 description 2
229930182830 galactose Natural products 0.000 description 2
210000004602 germ cell Anatomy 0.000 description 2
230000013595 glycosylation Effects 0.000 description 2
210000002216 heart Anatomy 0.000 description 2
239000001307 helium Substances 0.000 description 2
229910052734 helium Inorganic materials 0.000 description 2
SWQJXJOGLNCZEY-UHFFFAOYSA-N helium atom Chemical compound [He] SWQJXJOGLNCZEY-UHFFFAOYSA-N 0.000 description 2
210000003958 hematopoietic stem cell Anatomy 0.000 description 2
ZSIAUFGUXNUGDI-UHFFFAOYSA-N hexan-1-ol Chemical compound CCCCCCO ZSIAUFGUXNUGDI-UHFFFAOYSA-N 0.000 description 2
125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 2
125000001165 hydrophobic group Chemical group 0.000 description 2
208000015181 infectious disease Diseases 0.000 description 2
238000002347 injection Methods 0.000 description 2
239000007924 injection Substances 0.000 description 2
238000005342 ion exchange Methods 0.000 description 2
238000004255 ion exchange chromatography Methods 0.000 description 2
235000021190 leftovers Nutrition 0.000 description 2
230000000670 limiting effect Effects 0.000 description 2
210000005229 liver cell Anatomy 0.000 description 2
125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
210000001161 mammalian embryo Anatomy 0.000 description 2
230000004060 metabolic process Effects 0.000 description 2
230000000813 microbial effect Effects 0.000 description 2
235000013336 milk Nutrition 0.000 description 2
210000004080 milk Anatomy 0.000 description 2
239000008267 milk Substances 0.000 description 2
CERZMXAJYMMUDR-UHFFFAOYSA-N neuraminic acid Natural products NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO CERZMXAJYMMUDR-UHFFFAOYSA-N 0.000 description 2
239000002751 oligonucleotide probe Substances 0.000 description 2
210000001672 ovary Anatomy 0.000 description 2
239000010452 phosphate Substances 0.000 description 2
229920002981 polyvinylidene fluoride Polymers 0.000 description 2
210000001236 prokaryotic cell Anatomy 0.000 description 2
238000000734 protein sequencing Methods 0.000 description 2
239000011541 reaction mixture Substances 0.000 description 2
238000010188 recombinant method Methods 0.000 description 2
230000009467 reduction Effects 0.000 description 2
230000001105 regulatory effect Effects 0.000 description 2
210000003660 reticulum Anatomy 0.000 description 2
238000010839 reverse transcription Methods 0.000 description 2
230000007017 scission Effects 0.000 description 2
238000012216 screening Methods 0.000 description 2
230000028327 secretion Effects 0.000 description 2
230000035945 sensitivity Effects 0.000 description 2
238000000926 separation method Methods 0.000 description 2
IHQKEDIOMGYHEB-UHFFFAOYSA-M sodium dimethylarsinate Chemical compound [Na+].C[As](C)([O-])=O IHQKEDIOMGYHEB-UHFFFAOYSA-M 0.000 description 2
238000010186 staining Methods 0.000 description 2
238000004885 tandem mass spectrometry Methods 0.000 description 2
238000012360 testing method Methods 0.000 description 2
229960002180 tetracycline Drugs 0.000 description 2
229930101283 tetracycline Natural products 0.000 description 2
235000019364 tetracycline Nutrition 0.000 description 2
150000003522 tetracyclines Chemical class 0.000 description 2
230000010474 transient expression Effects 0.000 description 2
GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 2
JJVXHDTWVIPRBZ-VKHMYHEASA-N (2r)-2-[carboxy(methyl)amino]-3-sulfanylpropanoic acid Chemical compound OC(=O)N(C)[C@@H](CS)C(O)=O JJVXHDTWVIPRBZ-VKHMYHEASA-N 0.000 description 1
RDEIXVOBVLKYNT-VQBXQJRRSA-N (2r,3r,4r,5r)-2-[(1s,2s,3r,4s,6r)-4,6-diamino-3-[(2r,3r,6s)-3-amino-6-(1-aminoethyl)oxan-2-yl]oxy-2-hydroxycyclohexyl]oxy-5-methyl-4-(methylamino)oxane-3,5-diol;(2r,3r,4r,5r)-2-[(1s,2s,3r,4s,6r)-4,6-diamino-3-[(2r,3r,6s)-3-amino-6-(aminomethyl)oxan-2-yl]o Chemical compound OS(O)(=O)=O.O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H](CC[C@@H](CN)O2)N)[C@@H](N)C[C@H]1N.O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H](CC[C@H](O2)C(C)N)N)[C@@H](N)C[C@H]1N.O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N RDEIXVOBVLKYNT-VQBXQJRRSA-N 0.000 description 1
102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
OSJPPGNTCRNQQC-UWTATZPHSA-N 3-phospho-D-glyceric acid Chemical compound OC(=O)[C@H](O)COP(O)(O)=O OSJPPGNTCRNQQC-UWTATZPHSA-N 0.000 description 1
YZZVIKDAOTXDEB-UHFFFAOYSA-N 4-(aminomethyl)-3-(5,7-difluoro-1,2,3,4-tetrahydronaphthalen-2-yl)-1h-imidazole-2-thione Chemical compound NCC1=CNC(=S)N1C1CC2=CC(F)=CC(F)=C2CC1 YZZVIKDAOTXDEB-UHFFFAOYSA-N 0.000 description 1
101710169336 5'-deoxyadenosine deaminase Proteins 0.000 description 1
OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 1
102100022900 Actin, cytoplasmic 1 Human genes 0.000 description 1
108010085238 Actins Proteins 0.000 description 1
102100036664 Adenosine deaminase Human genes 0.000 description 1
206010067484 Adverse reaction Diseases 0.000 description 1
SAHQGRZIQVEJPF-JXUBOQSCSA-N Ala-Thr-Lys Chemical compound C[C@H](N)C(=O)N[C@@H]([C@H](O)C)C(=O)N[C@H](C(O)=O)CCCCN SAHQGRZIQVEJPF-JXUBOQSCSA-N 0.000 description 1
108010088751 Albumins Proteins 0.000 description 1
102000009027 Albumins Human genes 0.000 description 1
101710187573 Alcohol dehydrogenase 2 Proteins 0.000 description 1
101710133776 Alcohol dehydrogenase class-3 Proteins 0.000 description 1
102100023635 Alpha-fetoprotein Human genes 0.000 description 1
108700023418 Amidases Proteins 0.000 description 1
108020005544 Antisense RNA Proteins 0.000 description 1
OMLWNBVRVJYMBQ-YUMQZZPRSA-N Arg-Arg Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O OMLWNBVRVJYMBQ-YUMQZZPRSA-N 0.000 description 1
SSZGOKWBHLOCHK-DCAQKATOSA-N Arg-Lys-Asn Chemical compound NC(=O)C[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CCCN=C(N)N SSZGOKWBHLOCHK-DCAQKATOSA-N 0.000 description 1
HCAUEJAQCXVQQM-ACZMJKKPSA-N Asn-Glu-Asp Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O HCAUEJAQCXVQQM-ACZMJKKPSA-N 0.000 description 1
HXWUJJADFMXNKA-BQBZGAKWSA-N Asn-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H](N)CC(N)=O HXWUJJADFMXNKA-BQBZGAKWSA-N 0.000 description 1
VZNOVQKGJQJOCS-SRVKXCTJSA-N Asp-Asp-Tyr Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O VZNOVQKGJQJOCS-SRVKXCTJSA-N 0.000 description 1
DWBZEJHQQIURML-IMJSIDKUSA-N Asp-Ser Chemical compound OC(=O)C[C@H](N)C(=O)N[C@@H](CO)C(O)=O DWBZEJHQQIURML-IMJSIDKUSA-N 0.000 description 1
102100023927 Asparagine synthetase [glutamine-hydrolyzing] Human genes 0.000 description 1
108010070255 Aspartate-ammonia ligase Proteins 0.000 description 1
241000972773 Aulopiformes Species 0.000 description 1
208000035404 Autolysis Diseases 0.000 description 1
244000063299 Bacillus subtilis Species 0.000 description 1
235000014469 Bacillus subtilis Nutrition 0.000 description 1
108700003860 Bacterial Genes Proteins 0.000 description 1
DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
102100026189 Beta-galactosidase Human genes 0.000 description 1
108091003079 Bovine Serum Albumin Proteins 0.000 description 1
206010006187 Breast cancer Diseases 0.000 description 1
208000026310 Breast neoplasm Diseases 0.000 description 1
TXCIAUNLDRJGJZ-UHFFFAOYSA-N CMP-N-acetyl neuraminic acid Natural products O1C(C(O)C(O)CO)C(NC(=O)C)C(O)CC1(C(O)=O)OP(O)(=O)OCC1C(O)C(O)C(N2C(N=C(N)C=C2)=O)O1 TXCIAUNLDRJGJZ-UHFFFAOYSA-N 0.000 description 1
TXCIAUNLDRJGJZ-BILDWYJOSA-N CMP-N-acetyl-beta-neuraminic acid Chemical compound O1[C@@H]([C@H](O)[C@H](O)CO)[C@H](NC(=O)C)[C@@H](O)C[C@]1(C(O)=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(N=C(N)C=C2)=O)O1 TXCIAUNLDRJGJZ-BILDWYJOSA-N 0.000 description 1
101100268670 Caenorhabditis elegans acc-3 gene Proteins 0.000 description 1
101100492584 Caenorhabditis elegans ast-1 gene Proteins 0.000 description 1
OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 1
108010067225 Cell Adhesion Molecules Proteins 0.000 description 1
102000016289 Cell Adhesion Molecules Human genes 0.000 description 1
206010057248 Cell death Diseases 0.000 description 1
241000867607 Chlorocebus sabaeus Species 0.000 description 1
108700010070 Codon Usage Proteins 0.000 description 1
229940126062 Compound A Drugs 0.000 description 1
108091035707 Consensus sequence Proteins 0.000 description 1
241000699800 Cricetinae Species 0.000 description 1
241000699802 Cricetulus griseus Species 0.000 description 1
101150074155 DHFR gene Proteins 0.000 description 1
102000012410 DNA Ligases Human genes 0.000 description 1
108010061982 DNA Ligases Proteins 0.000 description 1
108010017826 DNA Polymerase I Proteins 0.000 description 1
102000004594 DNA Polymerase I Human genes 0.000 description 1
230000004544 DNA amplification Effects 0.000 description 1
108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
108090000204 Dipeptidase 1 Proteins 0.000 description 1
206010059866 Drug resistance Diseases 0.000 description 1
108010024212 E-Selectin Proteins 0.000 description 1
102100023471 E-selectin Human genes 0.000 description 1
241000196324 Embryophyta Species 0.000 description 1
241000305071 Enterobacterales Species 0.000 description 1
101710146739 Enterotoxin Proteins 0.000 description 1
YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
241001522878 Escherichia coli B Species 0.000 description 1
241001302584 Escherichia coli str. K-12 substr. W3110 Species 0.000 description 1
LFQSCWFLJHTTHZ-UHFFFAOYSA-N EtOH Substances CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
108700024394 Exon Proteins 0.000 description 1
108060002716 Exonuclease Proteins 0.000 description 1
102100026149 Fibroblast growth factor receptor-like 1 Human genes 0.000 description 1
102000006471 Fucosyltransferases Human genes 0.000 description 1
108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
CBEUFCJRFNZMCU-SRVKXCTJSA-N Glu-Met-Leu Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(C)C)C(O)=O CBEUFCJRFNZMCU-SRVKXCTJSA-N 0.000 description 1
ZZJVYSAQQMDIRD-UWVGGRQHSA-N Gly-Pro-His Chemical compound NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1cnc[nH]1)C(O)=O ZZJVYSAQQMDIRD-UWVGGRQHSA-N 0.000 description 1
239000004471 Glycine Substances 0.000 description 1
208000009889 Herpes Simplex Diseases 0.000 description 1
NLDMNSXOCDLTTB-UHFFFAOYSA-N Heterophylliin A Natural products O1C2COC(=O)C3=CC(O)=C(O)C(O)=C3C3=C(O)C(O)=C(O)C=C3C(=O)OC2C(OC(=O)C=2C=C(O)C(O)=C(O)C=2)C(O)C1OC(=O)C1=CC(O)=C(O)C(O)=C1 NLDMNSXOCDLTTB-UHFFFAOYSA-N 0.000 description 1
102000005548 Hexokinase Human genes 0.000 description 1
108700040460 Hexokinases Proteins 0.000 description 1
RXVOMIADLXPJGW-GUBZILKMSA-N His-Asp-Glu Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O RXVOMIADLXPJGW-GUBZILKMSA-N 0.000 description 1
101100066624 Homo sapiens FGFRL1 gene Proteins 0.000 description 1
101001050487 Homo sapiens IST1 homolog Proteins 0.000 description 1
101000622137 Homo sapiens P-selectin Proteins 0.000 description 1
101000835745 Homo sapiens Teratocarcinoma-derived growth factor 1 Proteins 0.000 description 1
241000701024 Human betaherpesvirus 5 Species 0.000 description 1
102100023423 IST1 homolog Human genes 0.000 description 1
ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical group C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 description 1
AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical group CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
125000003440 L-leucyl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])C(C([H])([H])[H])([H])C([H])([H])[H] 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
COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
102000004407 Lactalbumin Human genes 0.000 description 1
108090000942 Lactalbumin Proteins 0.000 description 1
239000000232 Lipid Bilayer Substances 0.000 description 1
GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
108010052285 Membrane Proteins Proteins 0.000 description 1
108010093077 N-Acetylglucosaminyltransferases Proteins 0.000 description 1
102000002493 N-Acetylglucosaminyltransferases Human genes 0.000 description 1
125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
101800000135 N-terminal protein Proteins 0.000 description 1
101150096752 NCAM1 gene Proteins 0.000 description 1
108010006232 Neuraminidase Proteins 0.000 description 1
102000005348 Neuraminidase Human genes 0.000 description 1
108700020497 Nucleopolyhedrovirus polyhedrin Proteins 0.000 description 1
102000052812 Ornithine decarboxylases Human genes 0.000 description 1
108700005126 Ornithine decarboxylases Proteins 0.000 description 1
101800001452 P1 proteinase Proteins 0.000 description 1
238000012408 PCR amplification Methods 0.000 description 1
238000010222 PCR analysis Methods 0.000 description 1
108010067372 Pancreatic elastase Proteins 0.000 description 1
102000016387 Pancreatic elastase Human genes 0.000 description 1
241000282376 Panthera tigris Species 0.000 description 1
108091036407 Polyadenylation Proteins 0.000 description 1
239000004952 Polyamide Substances 0.000 description 1
ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
102000001253 Protein Kinase Human genes 0.000 description 1
241000589516 Pseudomonas Species 0.000 description 1
108091034057 RNA (poly(A)) Proteins 0.000 description 1
238000002123 RNA extraction Methods 0.000 description 1
239000013614 RNA sample Substances 0.000 description 1
101100019711 Rattus norvegicus Camk1 gene Proteins 0.000 description 1
101100194625 Rattus norvegicus Rgs19 gene Proteins 0.000 description 1
108091028664 Ribonucleotide Proteins 0.000 description 1
241000235070 Saccharomyces Species 0.000 description 1
101100221606 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) COS7 gene Proteins 0.000 description 1
241000607142 Salmonella Species 0.000 description 1
108090000184 Selectins Proteins 0.000 description 1
102000003800 Selectins Human genes 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
BRKHVZNDAOMAHX-BIIVOSGPSA-N Ser-Ala-Pro Chemical compound C[C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](CO)N BRKHVZNDAOMAHX-BIIVOSGPSA-N 0.000 description 1
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
241000607720 Serratia Species 0.000 description 1
DSGIVWSDDRDJIO-ZXXMMSQZSA-N Thr-Thr Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(O)=O DSGIVWSDDRDJIO-ZXXMMSQZSA-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
108090000340 Transaminases Proteins 0.000 description 1
DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 1
GDPDVIBHJDFRFD-RNXOBYDBSA-N Trp-Tyr-Tyr Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O GDPDVIBHJDFRFD-RNXOBYDBSA-N 0.000 description 1
108091005956 Type II transmembrane proteins Proteins 0.000 description 1
GVJUTBOZZBTBIG-AVGNSLFASA-N Val-Lys-Arg Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N GVJUTBOZZBTBIG-AVGNSLFASA-N 0.000 description 1
IXKSXJFAGXLQOQ-XISFHERQSA-N WHWLQLKPGQPMY Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 IXKSXJFAGXLQOQ-XISFHERQSA-N 0.000 description 1
238000010521 absorption reaction Methods 0.000 description 1
QPMSXSBEVQLBIL-CZRHPSIPSA-N ac1mix0p Chemical compound C1=CC=C2N(C[C@H](C)CN(C)C)C3=CC(OC)=CC=C3SC2=C1.O([C@H]1[C@]2(OC)C=CC34C[C@@H]2[C@](C)(O)CCC)C2=C5[C@]41CCN(C)[C@@H]3CC5=CC=C2O QPMSXSBEVQLBIL-CZRHPSIPSA-N 0.000 description 1
238000009825 accumulation Methods 0.000 description 1
230000009471 action Effects 0.000 description 1
239000000654 additive Substances 0.000 description 1
230000006838 adverse reaction Effects 0.000 description 1
238000001261 affinity purification Methods 0.000 description 1
230000029936 alkylation Effects 0.000 description 1
238000005804 alkylation reaction Methods 0.000 description 1
WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 1
108010026331 alpha-Fetoproteins Proteins 0.000 description 1
NIGUVXFURDGQKZ-UQTBNESHSA-N alpha-Neup5Ac-(2->3)-beta-D-Galp-(1->4)-[alpha-L-Fucp-(1->3)]-beta-D-GlcpNAc Chemical compound O[C@H]1[C@H](O)[C@H](O)[C@H](C)O[C@H]1O[C@H]1[C@H](O[C@H]2[C@@H]([C@@H](O[C@]3(O[C@H]([C@H](NC(C)=O)[C@@H](O)C3)[C@H](O)[C@H](O)CO)C(O)=O)[C@@H](O)[C@@H](CO)O2)O)[C@@H](CO)O[C@@H](O)[C@@H]1NC(C)=O NIGUVXFURDGQKZ-UQTBNESHSA-N 0.000 description 1
102000005922 amidase Human genes 0.000 description 1
125000003277 amino group Chemical group 0.000 description 1
210000004102 animal cell Anatomy 0.000 description 1
239000007864 aqueous solution Substances 0.000 description 1
108010068380 arginylarginine Proteins 0.000 description 1
238000003149 assay kit Methods 0.000 description 1
244000052616 bacterial pathogen Species 0.000 description 1
108010058966 bacteriophage T7 induced DNA polymerase Proteins 0.000 description 1
108010051210 beta-Fructofuranosidase Proteins 0.000 description 1
IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
108010057005 beta-galactoside alpha-2,3-sialyltransferase Proteins 0.000 description 1
102000006635 beta-lactamase Human genes 0.000 description 1
GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 1
239000003150 biochemical marker Substances 0.000 description 1
230000008827 biological function Effects 0.000 description 1
230000033228 biological regulation Effects 0.000 description 1
230000005540 biological transmission Effects 0.000 description 1
210000002459 blastocyst Anatomy 0.000 description 1
230000000903 blocking effect Effects 0.000 description 1
229940098773 bovine serum albumin Drugs 0.000 description 1
210000005013 brain tissue Anatomy 0.000 description 1
210000000481 breast Anatomy 0.000 description 1
RDHPKYGYEGBMSE-UHFFFAOYSA-N bromoethane Chemical compound CCBr RDHPKYGYEGBMSE-UHFFFAOYSA-N 0.000 description 1
239000007853 buffer solution Substances 0.000 description 1
210000004900 c-terminal fragment Anatomy 0.000 description 1
238000010804 cDNA synthesis Methods 0.000 description 1
238000010805 cDNA synthesis kit Methods 0.000 description 1
239000007978 cacodylate buffer Substances 0.000 description 1
239000011575 calcium Substances 0.000 description 1
229910052791 calcium Inorganic materials 0.000 description 1
239000001506 calcium phosphate Substances 0.000 description 1
229910000389 calcium phosphate Inorganic materials 0.000 description 1
235000011010 calcium phosphates Nutrition 0.000 description 1
229940041514 candida albicans extract Drugs 0.000 description 1
239000004202 carbamide Substances 0.000 description 1
235000011089 carbon dioxide Nutrition 0.000 description 1
125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 description 1
239000000969 carrier Substances 0.000 description 1
238000006555 catalytic reaction Methods 0.000 description 1
239000006143 cell culture medium Substances 0.000 description 1
230000022131 cell cycle Effects 0.000 description 1
210000002421 cell wall Anatomy 0.000 description 1
230000019522 cellular metabolic process Effects 0.000 description 1
239000001913 cellulose Substances 0.000 description 1
229920002678 cellulose Polymers 0.000 description 1
238000005119 centrifugation Methods 0.000 description 1
208000019065 cervical carcinoma Diseases 0.000 description 1
230000008859 change Effects 0.000 description 1
238000007385 chemical modification Methods 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
238000004587 chromatography analysis Methods 0.000 description 1
230000002759 chromosomal effect Effects 0.000 description 1
210000001072 colon Anatomy 0.000 description 1
239000003184 complementary RNA Substances 0.000 description 1
238000007796 conventional method Methods 0.000 description 1
108700010903 cytomegalovirus proteins Proteins 0.000 description 1
210000000805 cytoplasm Anatomy 0.000 description 1
210000005220 cytoplasmic tail Anatomy 0.000 description 1
RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 1
230000034994 death Effects 0.000 description 1
238000006731 degradation reaction Methods 0.000 description 1
230000000593 degrading effect Effects 0.000 description 1
238000004925 denaturation Methods 0.000 description 1
230000036425 denaturation Effects 0.000 description 1
KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical group C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
229960003964 deoxycholic acid Drugs 0.000 description 1
KXGVEGMKQFWNSR-UHFFFAOYSA-N deoxycholic acid Natural products C1CC2CC(O)CCC2(C)C2C1C1CCC(C(CCC(O)=O)C)C1(C)C(O)C2 KXGVEGMKQFWNSR-UHFFFAOYSA-N 0.000 description 1
239000005547 deoxyribonucleotide Substances 0.000 description 1
125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
238000013461 design Methods 0.000 description 1
206010012601 diabetes mellitus Diseases 0.000 description 1
238000011026 diafiltration Methods 0.000 description 1
229910003460 diamond Inorganic materials 0.000 description 1
239000010432 diamond Substances 0.000 description 1
238000010790 dilution Methods 0.000 description 1
239000012895 dilution Substances 0.000 description 1
239000006185 dispersion Substances 0.000 description 1
238000010494 dissociation reaction Methods 0.000 description 1
230000005593 dissociations Effects 0.000 description 1
238000009510 drug design Methods 0.000 description 1
238000007877 drug screening Methods 0.000 description 1
238000001035 drying Methods 0.000 description 1
238000004070 electrodeposition Methods 0.000 description 1
238000004520 electroporation Methods 0.000 description 1
210000002472 endoplasmic reticulum Anatomy 0.000 description 1
210000002889 endothelial cell Anatomy 0.000 description 1
230000003511 endothelial effect Effects 0.000 description 1
239000000147 enterotoxin Substances 0.000 description 1
231100000655 enterotoxin Toxicity 0.000 description 1
230000007613 environmental effect Effects 0.000 description 1
238000009585 enzyme analysis Methods 0.000 description 1
238000012869 ethanol precipitation Methods 0.000 description 1
238000011156 evaluation Methods 0.000 description 1
230000007717 exclusion Effects 0.000 description 1
102000013165 exonuclease Human genes 0.000 description 1
210000003722 extracellular fluid Anatomy 0.000 description 1
230000002538 fungal effect Effects 0.000 description 1
239000007789 gas Substances 0.000 description 1
238000010363 gene targeting Methods 0.000 description 1
238000007429 general method Methods 0.000 description 1
238000010353 genetic engineering Methods 0.000 description 1
108060003196 globin Proteins 0.000 description 1
102000018146 globin Human genes 0.000 description 1
125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 1
102000005396 glutamine synthetase Human genes 0.000 description 1
108020002326 glutamine synthetase Proteins 0.000 description 1
108010042598 glutamyl-aspartyl-glycine Proteins 0.000 description 1
102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 1
108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 1
230000002414 glycolytic effect Effects 0.000 description 1
238000006206 glycosylation reaction Methods 0.000 description 1
239000006451 grace's insect medium Substances 0.000 description 1
239000008187 granular material Substances 0.000 description 1
239000003102 growth factor Substances 0.000 description 1
230000003394 haemopoietic effect Effects 0.000 description 1
208000006454 hepatitis Diseases 0.000 description 1
238000004128 high performance liquid chromatography Methods 0.000 description 1
230000001900 immune effect Effects 0.000 description 1
230000006698 induction Effects 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
239000003999 initiator Substances 0.000 description 1
230000000977 initiatory effect Effects 0.000 description 1
230000010354 integration Effects 0.000 description 1
230000003993 interaction Effects 0.000 description 1
239000001573 invertase Substances 0.000 description 1
235000011073 invertase Nutrition 0.000 description 1
239000003456 ion exchange resin Substances 0.000 description 1
229920003303 ion-exchange polymer Polymers 0.000 description 1
238000000752 ionisation method Methods 0.000 description 1
AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Chemical group CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
229960000310 isoleucine Drugs 0.000 description 1
125000000741 isoleucyl group Chemical group [H]N([H])C(C(C([H])([H])[H])C([H])([H])C([H])([H])[H])C(=O)O* 0.000 description 1
229950003188 isovaleryl diethylamide Drugs 0.000 description 1
230000003902 lesion Effects 0.000 description 1
150000002632 lipids Chemical class 0.000 description 1
239000007788 liquid Substances 0.000 description 1
229940040511 liver extract Drugs 0.000 description 1
238000011068 loading method Methods 0.000 description 1
210000004072 lung Anatomy 0.000 description 1
210000005265 lung cell Anatomy 0.000 description 1
229920002521 macromolecule Polymers 0.000 description 1
230000014759 maintenance of location Effects 0.000 description 1
210000003622 mature neutrocyte Anatomy 0.000 description 1
230000001404 mediated effect Effects 0.000 description 1
238000002844 melting Methods 0.000 description 1
230000008018 melting Effects 0.000 description 1
MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
WSFSSNUMVMOOMR-NJFSPNSNSA-N methanone Chemical compound O=[14CH2] WSFSSNUMVMOOMR-NJFSPNSNSA-N 0.000 description 1
229930182817 methionine Natural products 0.000 description 1
YACKEPLHDIMKIO-UHFFFAOYSA-N methylphosphonic acid Chemical group CP(O)(O)=O YACKEPLHDIMKIO-UHFFFAOYSA-N 0.000 description 1
244000005700 microbiome Species 0.000 description 1
238000000520 microinjection Methods 0.000 description 1
108091005601 modified peptides Proteins 0.000 description 1
210000001616 monocyte Anatomy 0.000 description 1
230000036457 multidrug resistance Effects 0.000 description 1
210000000653 nervous system Anatomy 0.000 description 1
210000002569 neuron Anatomy 0.000 description 1
210000000440 neutrophil Anatomy 0.000 description 1
230000002611 ovarian Effects 0.000 description 1
230000001590 oxidative effect Effects 0.000 description 1
238000004806 packaging method and process Methods 0.000 description 1
238000012856 packing Methods 0.000 description 1
238000004816 paper chromatography Methods 0.000 description 1
ISWSIDIOOBJBQZ-UHFFFAOYSA-N phenol group Chemical group C1(=CC=CC=C1)O ISWSIDIOOBJBQZ-UHFFFAOYSA-N 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
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
239000008363 phosphate buffer Substances 0.000 description 1
125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 1
230000007505 plaque formation Effects 0.000 description 1
239000013600 plasmid vector Substances 0.000 description 1
238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
230000008488 polyadenylation Effects 0.000 description 1
229920002647 polyamide Polymers 0.000 description 1
238000006116 polymerization reaction Methods 0.000 description 1
230000006267 polysialylation Effects 0.000 description 1
229920000136 polysorbate Polymers 0.000 description 1
239000011148 porous material Substances 0.000 description 1
230000001323 posttranslational effect Effects 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
239000002243 precursor Substances 0.000 description 1
239000002987 primer (paints) Substances 0.000 description 1
230000009465 prokaryotic expression Effects 0.000 description 1
AAEVYOVXGOFMJO-UHFFFAOYSA-N prometryn Chemical compound CSC1=NC(NC(C)C)=NC(NC(C)C)=N1 AAEVYOVXGOFMJO-UHFFFAOYSA-N 0.000 description 1
QMLAXRXNTUYJMM-UHFFFAOYSA-N propane-1,2,3-triol;3-sulfanylpropane-1,2-diol Chemical compound OCC(O)CO.OCC(O)CS QMLAXRXNTUYJMM-UHFFFAOYSA-N 0.000 description 1
NQCBIMOYRRMVNA-UHFFFAOYSA-N propane-1,2,3-triol;hydrochloride Chemical compound Cl.OCC(O)CO NQCBIMOYRRMVNA-UHFFFAOYSA-N 0.000 description 1
108060006633 protein kinase Proteins 0.000 description 1
230000006337 proteolytic cleavage Effects 0.000 description 1
230000005588 protonation Effects 0.000 description 1
210000001938 protoplast Anatomy 0.000 description 1
230000002285 radioactive effect Effects 0.000 description 1
239000002994 raw material Substances 0.000 description 1
108020003175 receptors Proteins 0.000 description 1
102000005962 receptors Human genes 0.000 description 1
230000006798 recombination Effects 0.000 description 1
238000005215 recombination Methods 0.000 description 1
230000002829 reductive effect Effects 0.000 description 1
238000011160 research Methods 0.000 description 1
238000004007 reversed phase HPLC Methods 0.000 description 1
239000002336 ribonucleotide Substances 0.000 description 1
125000002652 ribonucleotide group Chemical group 0.000 description 1
235000019515 salmon Nutrition 0.000 description 1
229920006395 saturated elastomer Polymers 0.000 description 1
230000028043 self proteolysis Effects 0.000 description 1
125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
210000000717 sertoli cell Anatomy 0.000 description 1
230000035939 shock Effects 0.000 description 1
230000009450 sialylation Effects 0.000 description 1
238000002741 site-directed mutagenesis Methods 0.000 description 1
210000000813 small intestine Anatomy 0.000 description 1
AGDSCTQQXMDDCV-UHFFFAOYSA-M sodium;2-iodoacetate Chemical compound [Na+].[O-]C(=O)CI AGDSCTQQXMDDCV-UHFFFAOYSA-M 0.000 description 1
239000007787 solid Substances 0.000 description 1
210000000952 spleen Anatomy 0.000 description 1
238000010561 standard procedure Methods 0.000 description 1
101150080727 stx gene Proteins 0.000 description 1
210000001913 submandibular gland Anatomy 0.000 description 1
150000008163 sugars Chemical group 0.000 description 1
238000011191 terminal modification Methods 0.000 description 1
230000001225 therapeutic effect Effects 0.000 description 1
125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 1
229940104230 thymidine Drugs 0.000 description 1
102000014898 transaminase activity proteins Human genes 0.000 description 1
230000005030 transcription termination Effects 0.000 description 1
230000007704 transition Effects 0.000 description 1
230000017105 transposition Effects 0.000 description 1
QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
239000001226 triphosphate Substances 0.000 description 1
235000011178 triphosphate Nutrition 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
101150108727 trpl gene Proteins 0.000 description 1
108010087967 type I signal peptidase Proteins 0.000 description 1
241000701161 unidentified adenovirus Species 0.000 description 1
241000712461 unidentified influenza virus Species 0.000 description 1
241001430294 unidentified retrovirus Species 0.000 description 1
125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
238000005406 washing Methods 0.000 description 1
239000002023 wood Substances 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1048—Glycosyltransferases (2.4)
- C12N9/1081—Glycosyltransferases (2.4) transferring other glycosyl groups (2.4.99)
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Zoology (AREA)
Genetics & Genomics (AREA)
Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Organic Chemistry (AREA)
Wood Science & Technology (AREA)
General Engineering & Computer Science (AREA)
Biomedical Technology (AREA)
Biotechnology (AREA)
Medicinal Chemistry (AREA)
Biochemistry (AREA)
Molecular Biology (AREA)
General Health & Medical Sciences (AREA)
Microbiology (AREA)
Enzymes And Modification Thereof (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Ceramic Products (AREA)
Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

BG99100A 1992-03-09 1994-10-07 Състави и методи за идентифициране и синтез насиалилтрансферази Expired - Lifetime BG62492B1 (bg)

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
US85035792A	1992-03-09	1992-03-09
US92536992A	1992-08-04	1992-08-04
PCT/US1993/002002 WO1993018157A1 (en)	1992-03-09	1993-03-09	Compositions and methods for the identification and synthesis of sialyltransferases

Publications (2)

Publication Number	Publication Date
BG99100A BG99100A (bg)	1995-05-31
BG62492B1 true BG62492B1 (bg)	1999-12-30

Family

ID=27126928

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
BG99100A Expired - Lifetime BG62492B1 (bg)	1992-03-09	1994-10-07	Състави и методи за идентифициране и синтез насиалилтрансферази

Country Status (17)

Country	Link
EP (1)	EP0632831B1 (cs)
JP (1)	JPH07505771A (cs)
KR (1)	KR100300467B1 (cs)
AT (1)	ATE228565T1 (cs)
AU (1)	AU668714B2 (cs)
BG (1)	BG62492B1 (cs)
CA (1)	CA2131703C (cs)
CZ (1)	CZ220494A3 (cs)
DE (1)	DE69332520T2 (cs)
DK (1)	DK0632831T3 (cs)
ES (1)	ES2191011T3 (cs)
FI (1)	FI119692B (cs)
HU (1)	HU219260B (cs)
NO (1)	NO314666B1 (cs)
NZ (1)	NZ251096A (cs)
SK (1)	SK108894A3 (cs)
WO (1)	WO1993018157A1 (cs)

Families Citing this family (26)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5384249A (en) *	1991-12-17	1995-01-24	Kyowa Hakko Kogyo Co., Ltd.	α2→3 sialyltransferase
US5849904A (en) *	1994-12-22	1998-12-15	Boehringer Mannheim Gmbh	Isolated nucleic acid molecules which hybridize to polysialyl transferases
AU692355B2 (en) *	1994-12-22	1998-06-04	Boehringer Mannheim Gmbh	Isolated polysialyl transferases, nucleic acid molecules coding therefor, methods of production and use
AUPN658795A0 (en) *	1995-11-15	1995-12-07	Commonwealth Scientific And Industrial Research Organisation	Method of producing alpha 2, 3 sialyltransferase
US6355255B1 (en) *	1998-12-07	2002-03-12	Regents Of The University Of Minnesota	Streptococcal C5a peptidase vaccine
AU755517B2 (en) *	1998-02-12	2002-12-12	Aventis Research & Technologies Gmbh & Co. Kg	Expression vector for the production of dead proteins
US6194178B1 (en)	1998-09-03	2001-02-27	Synsorb Biotech Inc.	Method for the production of sialylated oligosaccharides
WO2004099231A2 (en)	2003-04-09	2004-11-18	Neose Technologies, Inc.	Glycopegylation methods and proteins/peptides produced by the methods
US7214660B2 (en)	2001-10-10	2007-05-08	Neose Technologies, Inc.	Erythropoietin: remodeling and glycoconjugation of erythropoietin
US7173003B2 (en)	2001-10-10	2007-02-06	Neose Technologies, Inc.	Granulocyte colony stimulating factor: remodeling and glycoconjugation of G-CSF
WO2005012484A2 (en)	2003-07-25	2005-02-10	Neose Technologies, Inc.	Antibody-toxin conjugates
US20080305992A1 (en)	2003-11-24	2008-12-11	Neose Technologies, Inc.	Glycopegylated erythropoietin
US20080300173A1 (en)	2004-07-13	2008-12-04	Defrees Shawn	Branched Peg Remodeling and Glycosylation of Glucagon-Like Peptides-1 [Glp-1]
US20080318296A1 (en)	2004-07-21	2008-12-25	Inokuchi Jin-Ichi	Mutant Glycoprotein Resistant to Modification with Asparagine-Linked Sugar Chain
CA2585758C (en)	2004-10-29	2017-08-01	Neose Technologies, Inc.	Remodeling and glycopegylation of fibroblast growth factor (fgf)
NZ556436A (en)	2005-01-10	2010-11-26	Biogenerix Ag	Glycopegylated granulocyte colony stimulating factor
WO2006121569A2 (en)	2005-04-08	2006-11-16	Neose Technologies, Inc.	Compositions and methods for the preparation of protease resistant human growth hormone glycosylation mutants
US20070105755A1 (en)	2005-10-26	2007-05-10	Neose Technologies, Inc.	One pot desialylation and glycopegylation of therapeutic peptides
WO2007056191A2 (en)	2005-11-03	2007-05-18	Neose Technologies, Inc.	Nucleotide sugar purification using membranes
CN101516388B (zh)	2006-07-21	2012-10-31	诺和诺德公司	通过o-联糖基化序列的肽的糖基化
US8969532B2 (en)	2006-10-03	2015-03-03	Novo Nordisk A/S	Methods for the purification of polypeptide conjugates comprising polyalkylene oxide using hydrophobic interaction chromatography
NZ580030A (en)	2007-04-03	2012-06-29	Biogenerix Ag	Methods of treatment using glycopegylated g-csf
WO2008154639A2 (en)	2007-06-12	2008-12-18	Neose Technologies, Inc.	Improved process for the production of nucleotide sugars
EP2626079A3 (en)	2008-02-27	2014-03-05	Novo Nordisk A/S	Conjungated factor VIII molecules
CN102203122A (zh)	2008-11-05	2011-09-28	惠氏有限责任公司	用于预防β-溶血链球菌(BHS)疾病的多组分免疫原性组合物
AU2019211256A1 (en) *	2018-01-23	2020-08-06	Praveen BHOOPATHI	MDA-7/IL secretory variants and methods of use

Family Cites Families (5)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5059535A (en) *	1989-04-12	1991-10-22	Chembiomed, Ltd.	Process for the separation and purification of sialyl transferases
US5032519A (en) *	1989-10-24	1991-07-16	The Regents Of The Univ. Of California	Method for producing secretable glycosyltransferases and other Golgi processing enzymes
DE4028800A1 (de) *	1990-09-11	1992-03-12	Behringwerke Ag	Gentechnische sialylierung von glykoproteinen
SE9201544L (sv) *	1991-05-31	1992-12-01	Ciba Geigy Ag	Saett att framstaella glykosyltransferaser
GB2256197B (en) *	1991-05-31	1995-11-22	Ciba Geigy Ag	Yeast as host for expression of heterologous glycosyl transferase enzymes

1993
- 1993-03-09 AU AU37919/93A patent/AU668714B2/en not_active Expired
- 1993-03-09 WO PCT/US1993/002002 patent/WO1993018157A1/en active IP Right Grant
- 1993-03-09 ES ES93907244T patent/ES2191011T3/es not_active Expired - Lifetime
- 1993-03-09 CZ CZ942204A patent/CZ220494A3/cs unknown
- 1993-03-09 SK SK1088-94A patent/SK108894A3/sk unknown
- 1993-03-09 DE DE69332520T patent/DE69332520T2/de not_active Expired - Lifetime
- 1993-03-09 DK DK93907244T patent/DK0632831T3/da active
- 1993-03-09 JP JP5515911A patent/JPH07505771A/ja active Pending
- 1993-03-09 HU HU9402586A patent/HU219260B/hu unknown
- 1993-03-09 EP EP93907244A patent/EP0632831B1/en not_active Expired - Lifetime
- 1993-03-09 NZ NZ251096A patent/NZ251096A/en not_active IP Right Cessation
- 1993-03-09 CA CA002131703A patent/CA2131703C/en not_active Expired - Lifetime
- 1993-03-09 AT AT93907244T patent/ATE228565T1/de active
1994
- 1994-09-08 FI FI944136A patent/FI119692B/fi not_active IP Right Cessation
- 1994-09-08 NO NO19943323A patent/NO314666B1/no not_active IP Right Cessation
- 1994-09-09 KR KR940703163A patent/KR100300467B1/ko not_active Expired - Lifetime
- 1994-10-07 BG BG99100A patent/BG62492B1/bg not_active Expired - Lifetime

Also Published As

Publication number	Publication date
HU219260B (en)	2001-03-28
WO1993018157A1 (en)	1993-09-16
JPH07505771A (ja)	1995-06-29
HU9402586D0 (en)	1994-11-28
ATE228565T1 (de)	2002-12-15
NZ251096A (en)	1996-03-26
EP0632831B1 (en)	2002-11-27
EP0632831A1 (en)	1995-01-11
CA2131703A1 (en)	1993-09-16
DE69332520D1 (de)	2003-01-09
NO314666B1 (no)	2003-04-28
HUT69933A (en)	1995-09-28
NO943323L (no)	1994-11-01
FI944136A0 (fi)	1994-09-08
ES2191011T3 (es)	2003-09-01
CA2131703C (en)	2007-08-21
BG99100A (bg)	1995-05-31
DE69332520T2 (de)	2003-09-11
FI119692B (fi)	2009-02-13
FI944136L (fi)	1994-11-08
AU668714B2 (en)	1996-05-16
DK0632831T3 (da)	2003-03-24
NO943323D0 (no)	1994-09-08
AU3791993A (en)	1993-10-05
CZ220494A3 (en)	1995-03-15
SK108894A3 (en)	1995-07-11
KR100300467B1 (cs)	2001-10-22

Publication	Publication Date	Title
BG62492B1 (bg)	1999-12-30	Състави и методи за идентифициране и синтез насиалилтрансферази
US5858751A (en)	1999-01-12	Compositions and methods for producing sialyltransferases
US5962294A (en)	1999-10-05	Compositions and methods for the identification and synthesis of sialyltransferases
JP5590788B2 (ja)	2014-09-17	α−ガラクトシダーゼＡ欠損症の治療
Wen et al.	1992	Primary structure of Gal beta 1, 3 (4) GlcNAc alpha 2, 3-sialyltransferase determined by mass spectrometry sequence analysis and molecular cloning. Evidence for a protein motif in the sialyltransferase gene family.
ES2168101T5 (es)	2005-10-16	Clonacion y expresion de alfa-galactosidasa a biologicamente activa.
Jackson et al.	1990	Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum.
Tan et al.	1995	The human UDP‐N‐Acetylglucosamine: α‐6‐d‐Mannoside‐β‐1, 2‐N‐Acetylglucosaminyltransferase II Gene (MGAT2) Cloning of Genomic DNA, Localization to Chromosome 14q21, Expression in Insect Cells and Purification of the Recombinant Protein
NO329689B1 (no)	2010-11-29	Medisinske preparater til behandling av <alfa>-galaktosidase-A-defisiens
Harduin-Lepers et al.	2000	Cloning, expression and gene organization of a human Neu5Acα2–3Galβ1–3GalNAc α2, 6-sialyltransferase: hST6GalNAc IV
JPH11512933A (ja)	1999-11-09	キメラグリコシルトランスフェラーゼをコード化する改良された核酸
TOKI et al.	1997	Expression of stable human O-glycan core 2 β-1, 6-N-acetylglucosaminyltransferase in Sf9 insect cells
Lee et al.	1998	Cloning and expression of cDNA for a human Siaα2, 3Galβ1, 4GlcNA: α2, 8-sialyltransferase (hST8Sia III)
CA2483436A1 (en)	2003-11-06	N-acetylglucosaminyltransferase vb coding sequence, recombinant cells and methods
JP4101976B2 (ja)	2008-06-18	ヒト由来シアル酸転移酵素及びそれをコードするｄｎａ
SIGNAL	1995	High Mannose N-Glycans Processing Glycosidases
Feng	2003	Characterization and developmental studies on glucosidase II in the mouse mammary gland
VALLEJO-RUIZ et al.	2000	Cloning, expression and gene organization of a human Neu5Acα2–3Galβ1–3GalNAc α2, 6-sialyltransferase: hST6GalNAc IV1
JP2002204697A (ja)	2002-07-23	ヒトｄｎａリガーゼｉｖ
JP2006238810A (ja)	2006-09-14	糖鎖合成酵素
JP2002233366A (ja)	2002-08-20	ヒトデオキシシチジンキナーゼ２