FI78318C - Foerfarande foer framstaellning av kymosin. - Google Patents
Foerfarande foer framstaellning av kymosin. Download PDFInfo
- Publication number
- FI78318C FI78318C FI840468A FI840468A FI78318C FI 78318 C FI78318 C FI 78318C FI 840468 A FI840468 A FI 840468A FI 840468 A FI840468 A FI 840468A FI 78318 C FI78318 C FI 78318C
- Authority
- FI
- Finland
- Prior art keywords
- precursor
- chymosin
- insoluble
- denatured
- aqueous solution
- Prior art date
Links
- 108090000746 Chymosin Proteins 0.000 title claims description 85
- 229940080701 chymosin Drugs 0.000 title claims description 83
- GNOLWGAJQVLBSM-UHFFFAOYSA-N n,n,5,7-tetramethyl-1,2,3,4-tetrahydronaphthalen-1-amine Chemical compound C1=C(C)C=C2C(N(C)C)CCCC2=C1C GNOLWGAJQVLBSM-UHFFFAOYSA-N 0.000 title claims description 81
- 238000000034 method Methods 0.000 title claims description 21
- 230000008569 process Effects 0.000 title claims description 12
- 238000002360 preparation method Methods 0.000 title description 8
- 239000002243 precursor Substances 0.000 claims description 75
- 108090000623 proteins and genes Proteins 0.000 claims description 42
- 239000000243 solution Substances 0.000 claims description 19
- 241000588724 Escherichia coli Species 0.000 claims description 18
- 239000007864 aqueous solution Substances 0.000 claims description 16
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 claims description 15
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 13
- 239000004202 carbamide Substances 0.000 claims description 13
- 229960000789 guanidine hydrochloride Drugs 0.000 claims description 12
- 238000000605 extraction Methods 0.000 claims description 10
- 238000004925 denaturation Methods 0.000 claims description 8
- 230000036425 denaturation Effects 0.000 claims description 8
- 238000004519 manufacturing process Methods 0.000 claims description 4
- 239000007857 degradation product Substances 0.000 claims description 2
- 230000002441 reversible effect Effects 0.000 claims description 2
- 102000004169 proteins and genes Human genes 0.000 description 35
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 16
- 210000004027 cell Anatomy 0.000 description 12
- 108010064037 prorennin Proteins 0.000 description 12
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 9
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 8
- 229930182817 methionine Natural products 0.000 description 8
- 239000011780 sodium chloride Substances 0.000 description 8
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 7
- 239000008188 pellet Substances 0.000 description 7
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 239000012670 alkaline solution Substances 0.000 description 6
- 239000002585 base Substances 0.000 description 6
- 238000004090 dissolution Methods 0.000 description 6
- 239000000872 buffer Substances 0.000 description 5
- 239000000284 extract Substances 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 4
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 238000010790 dilution Methods 0.000 description 4
- 239000012895 dilution Substances 0.000 description 4
- 238000002474 experimental method Methods 0.000 description 4
- 239000000725 suspension Substances 0.000 description 4
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 3
- 239000007983 Tris buffer Substances 0.000 description 3
- 238000010306 acid treatment Methods 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 230000009089 cytolysis Effects 0.000 description 3
- 235000011187 glycerol Nutrition 0.000 description 3
- 229960004198 guanidine Drugs 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 238000006386 neutralization reaction Methods 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 238000004153 renaturation Methods 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 238000011282 treatment Methods 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 2
- 102000016943 Muramidase Human genes 0.000 description 2
- 108010014251 Muramidase Proteins 0.000 description 2
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 238000004220 aggregation Methods 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 238000011978 dissolution method Methods 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 230000005714 functional activity Effects 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000002386 leaching Methods 0.000 description 2
- 229960000274 lysozyme Drugs 0.000 description 2
- 235000010335 lysozyme Nutrition 0.000 description 2
- 239000004325 lysozyme Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 210000000496 pancreas Anatomy 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 238000005063 solubilization Methods 0.000 description 2
- 230000007928 solubilization Effects 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000010414 supernatant solution Substances 0.000 description 2
- 239000002699 waste material Substances 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 101000976075 Homo sapiens Insulin Proteins 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 238000001994 activation Methods 0.000 description 1
- 238000011276 addition treatment Methods 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 229960003964 deoxycholic acid Drugs 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound 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
- 238000000502 dialysis Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 239000011536 extraction buffer Substances 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 230000008823 permeabilization Effects 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 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
- C12N9/6478—Aspartic endopeptidases (3.4.23)
- C12N9/6481—Pepsins (3.4.23.1; 3.4.23.2; 3.4.23.3)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1136—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by reversible modification of the secondary, tertiary or quarternary structure, e.g. using denaturating or stabilising agents
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- General Chemical & Material Sciences (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Analytical Chemistry (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Crystallography & Structural Chemistry (AREA)
- General Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Saccharide Compounds (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CA404600 | 1982-06-07 | ||
| CA404600 | 1982-06-07 | ||
| GB8308234 | 1983-03-25 | ||
| GB838308234A GB8308234D0 (en) | 1983-03-25 | 1983-03-25 | Recovery of products produced by host organisms |
| PCT/GB1983/000152 WO1983004418A1 (en) | 1982-06-07 | 1983-06-07 | A process for the preparation of chymosin |
| GB8300152 | 1983-06-07 |
Publications (4)
| Publication Number | Publication Date |
|---|---|
| FI840468A0 FI840468A0 (fi) | 1984-02-06 |
| FI840468A7 FI840468A7 (fi) | 1984-02-06 |
| FI78318B FI78318B (fi) | 1989-03-31 |
| FI78318C true FI78318C (fi) | 1989-07-10 |
Family
ID=25669713
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| FI840468A FI78318C (fi) | 1982-06-07 | 1984-02-06 | Foerfarande foer framstaellning av kymosin. |
Country Status (10)
| Country | Link |
|---|---|
| EP (1) | EP0112849B1 (enExample) |
| JP (1) | JPS59500996A (enExample) |
| AU (1) | AU553017B2 (enExample) |
| DE (1) | DE3373676D1 (enExample) |
| DK (1) | DK49984A (enExample) |
| FI (1) | FI78318C (enExample) |
| GB (1) | GB2129810B (enExample) |
| IE (1) | IE55163B1 (enExample) |
| NZ (1) | NZ204477A (enExample) |
| WO (1) | WO1983004418A1 (enExample) |
Families Citing this family (31)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4663285A (en) * | 1981-01-06 | 1987-05-05 | The Public Health Laboratory Service Board | Chimeric plasmids |
| IE56372B1 (en) * | 1982-12-22 | 1991-07-03 | Genentech Inc | Microbially produced rennet methods for its production and plasmids used for its production |
| US4961938A (en) * | 1982-12-22 | 1990-10-09 | Genentech, Inc. | Preparation of cheese with rennin from recombinant microbial cells |
| US4512922A (en) * | 1982-12-22 | 1985-04-23 | Genentech, Inc. | Purification and activity assurance of precipitated heterologous proteins |
| US4511502A (en) * | 1982-12-22 | 1985-04-16 | Genentech, Inc. | Purification and activity assurance of precipitated heterologous proteins |
| US4620948A (en) * | 1982-12-22 | 1986-11-04 | Genentech, Inc. | Purification and activity assurance of precipitated heterologous proteins |
| JPS59162879A (ja) * | 1982-12-22 | 1984-09-13 | ジエネンテツク・インコ−ポレイテツド | 微生物により産生されるレンネツト、その産生及び再活性化方法並びにそれを使用するチ−ズの製造方法 |
| US4518526A (en) * | 1982-12-22 | 1985-05-21 | Genentech, Inc. | Purification and activity assurance of precipitated heterologous proteins |
| US4599197A (en) * | 1982-12-22 | 1986-07-08 | Genentech, Inc. | Purification and activity assurance of precipitated heterologous proteins |
| US5340926A (en) * | 1983-03-25 | 1994-08-23 | Celltech, Limited | Process for the recovery of recombinantly produced protein from insoluble aggregate |
| EP0122080B1 (en) * | 1983-03-25 | 1989-09-13 | Celltech Limited | A process for the production of a protein |
| EP0268743B1 (en) | 1983-03-25 | 1994-06-15 | Celltech Limited | A process for the production of a protein |
| US4935354A (en) * | 1983-07-14 | 1990-06-19 | Genentech, Inc. | Rennin from recombinant microbial cells for preparation of cheese |
| BG49718A3 (bg) * | 1983-07-15 | 1992-01-15 | Bio- Technology General Corp | Метод за получаване на полипептид със супероксиддисмутазна активност |
| US4721673A (en) * | 1983-09-01 | 1988-01-26 | Genex Corporation | Recovery and activation process for microbially produced calf prochymosin |
| IL74094A0 (en) * | 1984-01-23 | 1985-04-30 | Takeda Chemical Industries Ltd | Highly solubilised protein and production thereof |
| US5082775A (en) * | 1984-05-11 | 1992-01-21 | Berlex Laboratories, Inc. | Efficient process for isolating insoluble heterologous protein using non-ionic detergents |
| GB8414354D0 (en) * | 1984-06-05 | 1984-07-11 | Biogen Nv | Purifying protein |
| ES8800957A1 (es) * | 1985-02-22 | 1987-12-01 | Monsanto Co | Un metodo para la solubilizacion y renaturalizacion de proteina somatotropina |
| US4766205A (en) * | 1985-11-13 | 1988-08-23 | Beatrice Companies, Inc. | Method for isolation of recombinant polypeptides in biologically active forms |
| DE3611817A1 (de) * | 1986-04-08 | 1987-10-15 | Boehringer Mannheim Gmbh | Verfahren zur renaturierung von proteinen |
| US4705848A (en) * | 1986-06-02 | 1987-11-10 | International Minerals & Chemical Corp. | Isolation of bioactive, monomeric growth hormone |
| ATE78809T1 (de) | 1987-05-15 | 1992-08-15 | Univ Texas | Keramische zusammensetzungen und verfahren zu ihrer anwendung. |
| EP0301835A1 (en) * | 1987-07-29 | 1989-02-01 | Schering Biotech Corporation | Purification of human interleukin-4 expressed in Escherichia Coli |
| US5637566A (en) * | 1988-08-24 | 1997-06-10 | Southern Cross Biotech Pty. Ltd. | Method of improving carcass quality by administering growth hormone |
| US5064943A (en) * | 1988-12-16 | 1991-11-12 | American Cyanamid Company | Method for solubilization and naturation of somatotropin |
| AUPO005496A0 (en) * | 1996-05-24 | 1996-06-13 | Bresagen Limited | An interleukin-5 antagonist |
| US6465616B1 (en) | 1994-04-08 | 2002-10-15 | Bresagen Limited | Interleukin-5 antagonist |
| AU723413B2 (en) * | 1996-05-24 | 2000-08-24 | Bresagen Limited | An interleukin-5 antagonist |
| US6316240B1 (en) | 1999-01-25 | 2001-11-13 | Novozymes A/S | Recovery of a glycosidase or peptidase from a culture broth at high pH |
| DE10309691B4 (de) | 2003-02-28 | 2018-10-04 | Hans-Knöll-Institut für Naturstoff-Forschung e.V. | Gewinnung von löslichen Proteinen aus der Biomasse rekombinanter Mikroorganismen |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4350764A (en) * | 1980-03-10 | 1982-09-21 | The Regents Of The University Of California | Microbiological synthesis of beta endorphin |
| IE53517B1 (en) * | 1981-06-17 | 1988-12-07 | Celltech Ltd | Process for the production of a polypeptide |
-
1983
- 1983-06-07 AU AU16073/83A patent/AU553017B2/en not_active Ceased
- 1983-06-07 GB GB08401585A patent/GB2129810B/en not_active Expired
- 1983-06-07 WO PCT/GB1983/000152 patent/WO1983004418A1/en not_active Ceased
- 1983-06-07 EP EP83901829A patent/EP0112849B1/en not_active Expired
- 1983-06-07 NZ NZ204477A patent/NZ204477A/en unknown
- 1983-06-07 IE IE1341/83A patent/IE55163B1/en not_active IP Right Cessation
- 1983-06-07 JP JP58501900A patent/JPS59500996A/ja active Granted
- 1983-06-07 DE DE8383901829T patent/DE3373676D1/de not_active Expired
-
1984
- 1984-02-03 DK DK49984A patent/DK49984A/da not_active Application Discontinuation
- 1984-02-06 FI FI840468A patent/FI78318C/fi not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| DK49984D0 (da) | 1984-02-03 |
| FI78318B (fi) | 1989-03-31 |
| IE831341L (en) | 1983-12-07 |
| NZ204477A (en) | 1986-09-10 |
| JPH0472508B2 (enExample) | 1992-11-18 |
| EP0112849B1 (en) | 1987-09-16 |
| FI840468A0 (fi) | 1984-02-06 |
| DK49984A (da) | 1984-02-03 |
| GB2129810B (en) | 1985-09-18 |
| AU1607383A (en) | 1983-12-30 |
| AU553017B2 (en) | 1986-06-26 |
| JPS59500996A (ja) | 1984-06-07 |
| DE3373676D1 (en) | 1987-10-22 |
| FI840468A7 (fi) | 1984-02-06 |
| EP0112849A1 (en) | 1984-07-11 |
| WO1983004418A1 (en) | 1983-12-22 |
| GB2129810A (en) | 1984-05-23 |
| GB8401585D0 (en) | 1984-02-22 |
| IE55163B1 (en) | 1990-06-20 |
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