CH626402A5 - Process for immobilising proteins on a solid support - Google Patents

Process for immobilising proteins on a solid support Download PDF

Info

Publication number: CH626402A5
Authority: CH; Switzerland
Prior art keywords: washed; support; sepharose; solid; enzyme
Prior art date: 1975-04-09

Application number

CH423476A

Other languages

English (en)

Italian (it)

Inventor

Francesco Di Reegorio

Franco Morisi

Original Assignee

Snam Progetti

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.)

1975-04-09

Filing date

1976-04-05

Publication date

1981-11-13

1976-04-05 Application filed by Snam Progetti filed Critical Snam Progetti

1981-11-13 Publication of CH626402A5 publication Critical patent/CH626402A5/it

Links

239000007787 solid Substances 0.000 title claims description 25
102000004169 proteins and genes Human genes 0.000 title claims description 22
108090000623 proteins and genes Proteins 0.000 title claims description 22
238000000034 method Methods 0.000 title claims description 17
230000008569 process Effects 0.000 title claims description 7
AZQWKYJCGOJGHM-UHFFFAOYSA-N 1,4-benzoquinone Chemical compound O=C1C=CC(=O)C=C1 AZQWKYJCGOJGHM-UHFFFAOYSA-N 0.000 claims description 59
RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 claims description 6
ZRALSGWEFCBTJO-UHFFFAOYSA-N guanidine group Chemical group NC(=N)N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 claims description 3
150000001412 amines Chemical class 0.000 claims description 2
238000004925 denaturation Methods 0.000 claims description 2
230000036425 denaturation Effects 0.000 claims description 2
125000002887 hydroxy group Chemical group [H]O* 0.000 claims description 2
ISWSIDIOOBJBQZ-UHFFFAOYSA-N phenol group Chemical group C1(=CC=CC=C1)O ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 claims description 2
125000003396 thiol group Chemical group [H]S* 0.000 claims description 2
KAESVJOAVNADME-UHFFFAOYSA-N Pyrrole Chemical compound C=1C=CNC=1 KAESVJOAVNADME-UHFFFAOYSA-N 0.000 claims 2
102000004190 Enzymes Human genes 0.000 description 24
108090000790 Enzymes Proteins 0.000 description 24
229920002684 Sepharose Polymers 0.000 description 24
230000000694 effects Effects 0.000 description 18
102000004142 Trypsin Human genes 0.000 description 17
108090000631 Trypsin Proteins 0.000 description 17
239000012588 trypsin Substances 0.000 description 17
229940005561 1,4-benzoquinone Drugs 0.000 description 16
239000000872 buffer Substances 0.000 description 14
230000002255 enzymatic effect Effects 0.000 description 14
238000003756 stirring Methods 0.000 description 12
239000012064 sodium phosphate buffer Substances 0.000 description 11
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 11
239000007864 aqueous solution Substances 0.000 description 10
239000000203 mixture Substances 0.000 description 9
239000000243 solution Substances 0.000 description 9
238000005406 washing Methods 0.000 description 8
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
239000008363 phosphate buffer Substances 0.000 description 6
239000000126 substance Substances 0.000 description 6
239000000758 substrate Substances 0.000 description 6
108010073038 Penicillin Amidase Proteins 0.000 description 5
239000011541 reaction mixture Substances 0.000 description 5
108010093096 Immobilized Enzymes Proteins 0.000 description 4
JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 4
239000000047 product Substances 0.000 description 4
239000003643 water by type Substances 0.000 description 4
102000003992 Peroxidases Human genes 0.000 description 3
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
108040007629 peroxidase activity proteins Proteins 0.000 description 3
229920000642 polymer Polymers 0.000 description 3
239000011780 sodium chloride Substances 0.000 description 3
KETQAJRQOHHATG-UHFFFAOYSA-N 1,2-naphthoquinone Chemical compound C1=CC=C2C(=O)C(=O)C=CC2=C1 KETQAJRQOHHATG-UHFFFAOYSA-N 0.000 description 2
229940105324 1,2-naphthoquinone Drugs 0.000 description 2
RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 2
241000901842 Escherichia coli W Species 0.000 description 2
235000010469 Glycine max Nutrition 0.000 description 2
244000068988 Glycine max Species 0.000 description 2
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
101710162629 Trypsin inhibitor Proteins 0.000 description 2
229940122618 Trypsin inhibitor Drugs 0.000 description 2
239000003242 anti bacterial agent Substances 0.000 description 2
229940088710 antibiotic agent Drugs 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
238000004132 cross linking Methods 0.000 description 2
239000012847 fine chemical Substances 0.000 description 2
239000002638 heterogeneous catalyst Substances 0.000 description 2
239000003041 laboratory chemical Substances 0.000 description 2
DEQXHPXOGUSHDX-UHFFFAOYSA-N methylaminomethanetriol;hydrochloride Chemical compound Cl.CNC(O)(O)O DEQXHPXOGUSHDX-UHFFFAOYSA-N 0.000 description 2
229940056360 penicillin g Drugs 0.000 description 2
239000011535 reaction buffer Substances 0.000 description 2
238000001179 sorption measurement Methods 0.000 description 2
230000006641 stabilisation Effects 0.000 description 2
238000011105 stabilization Methods 0.000 description 2
DGQOCLATAPFASR-UHFFFAOYSA-N tetrahydroxy-1,4-benzoquinone Chemical compound OC1=C(O)C(=O)C(O)=C(O)C1=O DGQOCLATAPFASR-UHFFFAOYSA-N 0.000 description 2
LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
239000002753 trypsin inhibitor Substances 0.000 description 2
CPOBTYJRKAJERX-UHFFFAOYSA-N 3-ethyl-n-[(3-ethyl-1,3-benzothiazol-2-ylidene)amino]-1,3-benzothiazol-2-imine Chemical compound S1C2=CC=CC=C2N(CC)C1=NN=C1SC2=CC=CC=C2N1CC CPOBTYJRKAJERX-UHFFFAOYSA-N 0.000 description 1
LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 description 1
241000588724 Escherichia coli Species 0.000 description 1
CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
241000283973 Oryctolagus cuniculus Species 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
230000004913 activation Effects 0.000 description 1
239000000427 antigen Substances 0.000 description 1
102000036639 antigens Human genes 0.000 description 1
108091007433 antigens Proteins 0.000 description 1
OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 1
230000008901 benefit Effects 0.000 description 1
230000015572 biosynthetic process Effects 0.000 description 1
239000007853 buffer solution Substances 0.000 description 1
239000003054 catalyst Substances 0.000 description 1
238000005119 centrifugation Methods 0.000 description 1
238000007385 chemical modification Methods 0.000 description 1
239000007795 chemical reaction product Substances 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
238000000502 dialysis Methods 0.000 description 1
SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
239000002532 enzyme inhibitor Substances 0.000 description 1
239000005556 hormone Substances 0.000 description 1
229940088597 hormone Drugs 0.000 description 1
238000011534 incubation Methods 0.000 description 1
239000003112 inhibitor Substances 0.000 description 1
230000000977 initiatory effect Effects 0.000 description 1
238000002955 isolation Methods 0.000 description 1
239000007788 liquid Substances 0.000 description 1
239000012528 membrane Substances 0.000 description 1
238000002156 mixing Methods 0.000 description 1
229910000403 monosodium phosphate Inorganic materials 0.000 description 1
235000019799 monosodium phosphate Nutrition 0.000 description 1
238000011017 operating method Methods 0.000 description 1
229910000160 potassium phosphate Inorganic materials 0.000 description 1
239000008057 potassium phosphate buffer Substances 0.000 description 1
235000011009 potassium phosphates Nutrition 0.000 description 1
238000000746 purification Methods 0.000 description 1
-1 pyrrolic Chemical group 0.000 description 1
150000004053 quinones Chemical class 0.000 description 1
230000035484 reaction time Effects 0.000 description 1
238000000926 separation method Methods 0.000 description 1
AJPJDKMHJJGVTQ-UHFFFAOYSA-M sodium dihydrogen phosphate Chemical compound [Na+].OP(O)([O-])=O AJPJDKMHJJGVTQ-UHFFFAOYSA-M 0.000 description 1
239000001488 sodium phosphate Substances 0.000 description 1
239000012265 solid product Substances 0.000 description 1
239000010414 supernatant solution Substances 0.000 description 1
229920003169 water-soluble polymer Polymers 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
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6427—Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/44—Antibodies bound to carriers
- 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
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- 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
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/10—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a carbohydrate
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
- G01N33/54353—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals with ligand attached to the carrier via a chemical coupling agent

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Engineering & Computer Science (AREA)
Chemical & Material Sciences (AREA)
Bioinformatics & Cheminformatics (AREA)
Zoology (AREA)
Biomedical Technology (AREA)
Organic Chemistry (AREA)
Genetics & Genomics (AREA)
Wood Science & Technology (AREA)
Microbiology (AREA)
Immunology (AREA)
General Health & Medical Sciences (AREA)
Biotechnology (AREA)
Medicinal Chemistry (AREA)
Biochemistry (AREA)
Molecular Biology (AREA)
General Engineering & Computer Science (AREA)
Urology & Nephrology (AREA)
Hematology (AREA)
General Physics & Mathematics (AREA)
Pathology (AREA)
Analytical Chemistry (AREA)
Physics & Mathematics (AREA)
Food Science & Technology (AREA)
Cell Biology (AREA)
Mycology (AREA)
Pharmacology & Pharmacy (AREA)
Epidemiology (AREA)
Animal Behavior & Ethology (AREA)
Public Health (AREA)
Veterinary Medicine (AREA)
Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Enzymes And Modification Thereof (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)

CH423476A 1975-04-09 1976-04-05 Process for immobilising proteins on a solid support CH626402A5 (en)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
IT22140/75A IT1034957B (it)	1975-04-09	1975-04-09	Procedimento per la modifica chimica di sostanze proteichemezzi adatti allo scopo e procedimento per la preparazionedi questi

Publications (1)

Publication Number	Publication Date
CH626402A5 true CH626402A5 (en)	1981-11-13

Family

ID=11192081

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CH423476A CH626402A5 (en)	1975-04-09	1976-04-05	Process for immobilising proteins on a solid support

Country Status (20)

Country	Link
JP (1)	JPS51123884A (no)
AU (1)	AU508947B2 (no)
BE (1)	BE840450A (no)
CH (1)	CH626402A5 (no)
CS (1)	CS194238B2 (no)
DD (1)	DD123608A5 (no)
DE (1)	DE2615349C3 (no)
DK (1)	DK145676A (no)
FR (1)	FR2366303A1 (no)
GB (1)	GB1546237A (no)
HU (1)	HU175295B (no)
IL (1)	IL49356A (no)
IT (1)	IT1034957B (no)
LU (1)	LU74712A1 (no)
NL (1)	NL7603740A (no)
NO (1)	NO146332C (no)
SE (1)	SE7604136L (no)
TR (1)	TR18669A (no)
YU (1)	YU90576A (no)
ZA (1)	ZA761886B (no)

Families Citing this family (6)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
FR2334107A1 (fr) *	1975-12-05	1977-07-01	Pasteur Institut	Procede de couplage de substances biologiques par des liaisons covalentes
US4338398A (en) *	1979-03-20	1982-07-06	Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo	Immobilization of starch degrading enzymes
SE8006102L (sv) *	1980-09-02	1982-03-03	Gambro Ab	Sett att utvinna en peptidinnehallande forening samt medel for genomforande av settet
DE3130606C2 (de) *	1981-08-01	1985-03-21	Rolf Dr. 8700 Würzburg Siegel	Verfahren zur Isolierung von an der Antikörperbildung beteiligten Zellen
US4432895A (en) *	1982-11-24	1984-02-21	Hoffmann-La Roche Inc.	Monomeric interferons
DE10059720A1 (de)	2000-11-30	2002-06-06	Roche Diagnostics Gmbh	Verwendung intramolekular kovalent vernetzter Proteine als Bindepartner in Immunoassays

1975
- 1975-04-09 IT IT22140/75A patent/IT1034957B/it active
1976
- 1976-03-29 ZA ZA761886A patent/ZA761886B/xx unknown
- 1976-03-30 DK DK145676A patent/DK145676A/da not_active IP Right Cessation
- 1976-04-01 AU AU12551/76A patent/AU508947B2/en not_active Expired
- 1976-04-05 CH CH423476A patent/CH626402A5/it not_active IP Right Cessation
- 1976-04-05 GB GB13754/76A patent/GB1546237A/en not_active Expired
- 1976-04-06 TR TR18669A patent/TR18669A/xx unknown
- 1976-04-06 IL IL49356A patent/IL49356A/xx unknown
- 1976-04-07 FR FR7610089A patent/FR2366303A1/fr active Granted
- 1976-04-07 BE BE165896A patent/BE840450A/xx not_active IP Right Cessation
- 1976-04-07 DD DD192248A patent/DD123608A5/xx unknown
- 1976-04-07 LU LU74712A patent/LU74712A1/xx unknown
- 1976-04-07 NO NO761187A patent/NO146332C/no unknown
- 1976-04-08 DE DE2615349A patent/DE2615349C3/de not_active Expired
- 1976-04-08 CS CS762335A patent/CS194238B2/cs unknown
- 1976-04-08 YU YU00905/76A patent/YU90576A/xx unknown
- 1976-04-08 HU HU76SA2913A patent/HU175295B/hu unknown
- 1976-04-08 SE SE7604136A patent/SE7604136L/xx unknown
- 1976-04-08 NL NL7603740A patent/NL7603740A/xx not_active Application Discontinuation
- 1976-04-09 JP JP51039418A patent/JPS51123884A/ja active Pending

Also Published As

Publication number	Publication date
DE2615349C3 (de)	1979-02-08
AU1255176A (en)	1977-10-06
IT1034957B (it)	1979-10-10
BE840450A (fr)	1976-10-07
DK145676A (da)	1976-10-10
IL49356A0 (en)	1976-06-30
AU508947B2 (en)	1980-04-17
ZA761886B (en)	1977-03-30
GB1546237A (en)	1979-05-23
FR2366303B1 (no)	1980-01-11
NO146332B (no)	1982-06-01
TR18669A (tr)	1977-06-23
CS194238B2 (en)	1979-11-30
DE2615349B2 (de)	1978-06-15
NO146332C (no)	1982-09-08
SE7604136L (sv)	1976-10-10
LU74712A1 (no)	1976-11-11
NO761187L (no)	1976-10-12
YU90576A (en)	1983-04-30
DD123608A5 (no)	1977-01-05
HU175295B (hu)	1980-06-28
NL7603740A (nl)	1976-10-12
DE2615349A1 (de)	1976-10-14
IL49356A (en)	1980-03-31
FR2366303A1 (fr)	1978-04-28
JPS51123884A (en)	1976-10-28

Publication	Publication Date	Title
US3917527A (en)	1975-11-04	Hydrophobic chromatography
Papahadjopoulos et al.	1973	Role of cholesterol in membranes effects on phospholipid-protein interactions, membrane permeability and enzymatic activity
Cuatrecasas et al.	1971	[31] Affinity chromatography
Bayer et al.	1974	[20] Insolubilized biotin for the purification of avidin
Dills Jr et al.	1975	Purification of rabbit skeletal muscle protein kinase regulatory subunit using cyclic adenosine-3′: 5′-monophosphate affinity chromatography
JPH032560A (ja)	1991-01-08	新規なクロマトグラフィー用固定担体
Perry	1960	The chromatography of L-myosin on diethylaminoethylcellulose
US3983001A (en)	1976-09-28	Isolation of biologically active compounds by affinity chromatography
CN104277111A (zh)	2015-01-14	用于制备固定化蛋白质、多肽或寡肽的复合载体、制法及用途
Chang et al.	1991	Protein separation and purification in neat dimethyl sulfoxide
CH626402A5 (en)	1981-11-13	Process for immobilising proteins on a solid support
Kent et al.	1960	Immunochemically-active cross-linked polystyrene preparations
JPS5832591B2 (ja)	1983-07-14	ウロキナ−ゼの精製法
Steers Jr et al.	1974	[34] β-Galactosidase
JP2020065486A (ja)	2020-04-30	酵素固定化用担体および固定化酵素
Tu et al.	1972	Insolubilized D-amino acid oxidase: Properties and potential use
WO1996025425A1 (en)	1996-08-22	Purified tetanus toxoid and toxin
US3736230A (en)	1973-05-29	Process for producing 6-amino-penicillanic acid
Siegelman et al.	1976	Plastocyanin: Possible significance of quaternary structure
Lin et al.	1991	Two-step affinity chromatography. Model systems and an example using biotin-avidin binding and a fluoridolyzable linker
GB1449471A (en)	1976-09-15	Process for the manufacture of activated carriers for fixing amino compounds and carrier-bonded materials derived therefrom
EP0263484B1 (en)	1994-03-02	Method for isolation and purification of amylases, and adsorbents used for the same as well as devices for the isolation and purification
SU1419717A1 (ru)	1988-08-30	Способ получени биоспецифических адсорбентов дл выделени фибронектина и коллагеназ
US4268631A (en)	1981-05-19	Apoglucose oxidase preparation
Lenfeld et al.	1995	3, 5-Diiodo-L-tyrosine immobilized on bead cellulose

Legal Events

Date	Code	Title	Description
1982-05-28	PUE	Assignment	Owner name: ANIC S.P.A.
1985-12-31	PL	Patent ceased
2024-10-31	PL	Patent ceased