DK200001897A - Fremgangsmåde til aktivering af genteknologisk fremstillede, heterologe, disulfidbroer indeholdende eukaryotiske proteiner - Google Patents
Fremgangsmåde til aktivering af genteknologisk fremstillede, heterologe, disulfidbroer indeholdende eukaryotiske proteiner Download PDFInfo
- Publication number
- DK200001897A DK200001897A DK200001897A DKPA200001897A DK200001897A DK 200001897 A DK200001897 A DK 200001897A DK 200001897 A DK200001897 A DK 200001897A DK PA200001897 A DKPA200001897 A DK PA200001897A DK 200001897 A DK200001897 A DK 200001897A
- Authority
- DK
- Denmark
- Prior art keywords
- pref
- denaturing
- esp
- disulfide bridges
- eukaryotic proteins
- Prior art date
Links
- 238000000034 method Methods 0.000 title abstract description 21
- 230000003213 activating effect Effects 0.000 title abstract description 3
- 108090000623 proteins and genes Proteins 0.000 title description 10
- 102000004169 proteins and genes Human genes 0.000 title description 9
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 abstract description 9
- 239000003795 chemical substances by application Substances 0.000 abstract description 6
- 230000007420 reactivation Effects 0.000 abstract description 5
- 229960000789 guanidine hydrochloride Drugs 0.000 abstract description 4
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 abstract description 4
- 239000004475 Arginine Substances 0.000 abstract description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 abstract description 3
- 210000001236 prokaryotic cell Anatomy 0.000 abstract description 3
- 241000588724 Escherichia coli Species 0.000 abstract description 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 abstract description 2
- 241000589776 Pseudomonas putida Species 0.000 abstract description 2
- YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 abstract description 2
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 abstract 3
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 abstract 3
- 229960000187 tissue plasminogen activator Drugs 0.000 abstract 3
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 abstract 1
- 239000004202 carbamide Substances 0.000 abstract 1
- 230000006037 cell lysis Effects 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 8
- 150000001875 compounds Chemical class 0.000 description 4
- 229960003180 glutathione Drugs 0.000 description 4
- 108010024636 Glutathione Proteins 0.000 description 2
- 125000000217 alkyl group Chemical group 0.000 description 2
- 125000004432 carbon atom Chemical group C* 0.000 description 2
- 210000004027 cell Anatomy 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 150000002019 disulfides Chemical class 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 108010053070 Glutathione Disulfide Proteins 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000012062 aqueous buffer Substances 0.000 description 1
- 229960003121 arginine Drugs 0.000 description 1
- 229960003589 arginine hydrochloride Drugs 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 239000006185 dispersion Substances 0.000 description 1
- VHJLVAABSRFDPM-ZXZARUISSA-N dithioerythritol Chemical compound SC[C@H](O)[C@H](O)CS VHJLVAABSRFDPM-ZXZARUISSA-N 0.000 description 1
- 238000002270 exclusion chromatography Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 238000002604 ultrasonography Methods 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-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
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6456—Plasminogen activators
-
- 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)
- C12N9/6456—Plasminogen activators
- C12N9/6459—Plasminogen activators t-plasminogen activator (3.4.21.68), i.e. tPA
-
- 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
- C07K1/1133—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 redox-reactions involving cystein/cystin side chains
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/555—Interferons [IFN]
- C07K14/565—IFN-beta
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21069—Protein C activated (3.4.21.69)
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Wood Science & Technology (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Mechanical Treatment Of Semiconductor (AREA)
- Lubricants (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
Description
PATENTKRAV 1. Fremgangsmåde til aktivering af heterologe, disulfidbro-holdige eukaryotiske proteiner, fremstillet genteknologisk ved ekspression i prokaryotiske celler ved a) oplukning af de prokaryotiske celler, b) opløsning af de eukaryotiske proteiner under denaturerende og reducerende betingelser, c) fraskillelse af de reducerende/denaturerende midler, d) reaktivering under oxiderende betingelser ved e) omdannelse af de solubiliserede proteiners thiol-grupper til de blandede disulfider af protein og glutation ved tilsætning af GSSG under denaturerende betingelser, f) dannelse af aktivt protein ud fra de blandede disulfider ved en GSH-koncentration på 0,5 til 5 mmol/1, en pH-værdi på 7 til 10,5 og i nærværelse af en ikke-dena-turerende koncentration af et denatueringsmiddel. 2. Fremgangsmåde ifølge krav 1, kendetegnet ved, at man gennemfører ekspressionen i E. coli eller P. putida. 3. Fremgangmåde ifølge krav 1 eller 2, kendetegnet ved, at man i reaktiveringstrinnet som denatureringsmiddel anvender arginin, guanidin-hydrochlorid og/eller mindst en forbindelse med den almene formel R2-CO-NRRi (I), hvor R og R, er H eller alkyl med 1 til 4 C-atomer, og R2 er H eller NHR, eller alkyl med 1 til 3 C-atomer. 4. Fremgangsmåde ifølge krav 3, kendetegnet ved, at koncentrationen af arginin og/eller guanidin-hydrochlorid andrager 0,1 til 1,0 mol/1, navnlig 0,25 til 0,8 mol/1. 5. Fremgangsmåde ifølge krav 3, kendetegnet ved, at koncentrationen af forbindelsen med den almene formel I andrager 0,5 til 4 mol/1, navnlig 1 til 3,5 mol/1. 6. Fremgangsmåde ifølge ethvert af de foregående krav, kendetegnet ved, at der ved reaktiveringstrinnet arbejdes ved tilstedeværelse af et ikke-proteolytisk virksomt protein, navnlig ved tilstedeværelse af okseserumalbumin. 7. Fremgangsmåde ifølge ethvert af de foregående krav, kendetegnet ved, at man gennemfører celleoplukningen ved hjælp af ultralyd, højttryksdispersion eller Iysozym. 8. Fremgangsmåde ifølge krav 7, kendetegnet ved, at man gennemfører oplukningen i en fortyndet vandig pufferopløsning, navnlig i 0,1 mol/1 Tris, ved en neutral til svagt sur pH-værdi. 9. Fremgangsmåde ifølge ethvert af de foregående krav, kendetegnet ved, at man efter celleoplukningen fraskiller de uopløselige bestanddele. 10. Fremgangsmåde ifølge ethvert af de foregående krav, kendetegnet ved, at man gennemfører solubiliseringstrinnet ved alkalisk pH-værdi i nærværelse af et reduktionsmiddel fra mercaptogruppen og i nærværelse af et denatureringsmiddel. 11. Fremgangsmåde ifølge krav 10, kendetegnet ved, at man arbejder i nærværelse af guanidin-hydrochlorid og/eller forbindelser med den almene formel I som denatureringsmiddel. 12. Fremgangsmåde ifølge krav 11, kendetegnet ved, at koncentrationen af guanidindhydrochlorid andrager 6 mol/1, koncentration af forbindelser med den almene formel I andrager 8 mol/I. 13. Fremgangsmåde ifølge ethvert af kravene 10 til 12, kendetegnet ved, at man arbejder ved tilstedeværelse af DTE, β-mercaptoethanol, cystein eller GSH. 14. Fremgangsmåde ifølge ethvert af de foregående krav, kendetegnet ved, at man gennemfører rensning og fraskillelse af reduktions-, oxidations- eller denaturerings-midler ved hjælp af sterisk udelukkelseschromatografi eller dialyse. 15. Fremgangsmåde ifølge ethvert af de foregående krav, kendetegnet ved, at man efter reaktiveringstrinnet gennemfører et rensningstrin ved hjælp af dialyse. 16. Fremgangsmåde ifølge ethvert af kravene 1 til 15, k e n d e t e g n e t ved, at man som genteknologisk fremstillet eukaryotisk protein anvender t-PA. 17. Stimulerbar, ikke-glycosyleret tPA, opnået i overensstemmelse med fremgangsmåden ifølge ethvert af kravene 1 til 16. 18. Fremgangsmåde ifølge krav 6, kendetegnet ved, at man ved hjælp af ionbyt-terbehandling fraskiller det blandede disulfid af protein og glutathion fra ik-ke-modificeret protein.
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE19853537708 DE3537708A1 (de) | 1985-10-23 | 1985-10-23 | Verfahren zur aktivierung von t-pa nach expression in prokaryonten |
| DE3537708 | 1985-10-23 | ||
| DK198703203A DK175091B1 (da) | 1985-10-23 | 1987-06-23 | Fremgangsmåde til aktivering af genteknologisk fremstillede, heterologe, disulfidbro-holdige eukaryotiske proteiner efter ekspression i prokaryotiske celler |
| DK320387 | 1987-06-23 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| DK200001897A true DK200001897A (da) | 2000-12-18 |
| DK175109B1 DK175109B1 (da) | 2004-06-07 |
Family
ID=6284269
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK198703203A DK175091B1 (da) | 1985-10-23 | 1987-06-23 | Fremgangsmåde til aktivering af genteknologisk fremstillede, heterologe, disulfidbro-holdige eukaryotiske proteiner efter ekspression i prokaryotiske celler |
| DK200001897A DK175109B1 (da) | 1985-10-23 | 2000-12-18 | Fremgangsmåde til aktivering af genteknologisk fremstillede, heterologe, disulfidbroer indeholdende eukaryotiske proteiner efter ekspression i prokaryotiske celler |
Family Applications Before (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK198703203A DK175091B1 (da) | 1985-10-23 | 1987-06-23 | Fremgangsmåde til aktivering af genteknologisk fremstillede, heterologe, disulfidbro-holdige eukaryotiske proteiner efter ekspression i prokaryotiske celler |
Country Status (26)
| Country | Link |
|---|---|
| EP (3) | EP0219874B1 (da) |
| JP (2) | JPH0728745B2 (da) |
| KR (1) | KR900009139B1 (da) |
| AT (2) | ATE131489T1 (da) |
| AU (2) | AU590029B2 (da) |
| CA (1) | CA1329157C (da) |
| CZ (1) | CZ280727B6 (da) |
| DD (1) | DD260517A5 (da) |
| DE (3) | DE3537708A1 (da) |
| DK (2) | DK175091B1 (da) |
| ES (2) | ES2020498T3 (da) |
| FI (2) | FI94050C (da) |
| GR (2) | GR920300062T1 (da) |
| HK (2) | HK153496A (da) |
| HR (1) | HRP921075B1 (da) |
| HU (2) | HU204855B (da) |
| IE (1) | IE62634B1 (da) |
| IL (1) | IL80325A (da) |
| PT (1) | PT83609B (da) |
| SI (1) | SI8611796B (da) |
| SK (1) | SK752686A3 (da) |
| SU (1) | SU1607689A3 (da) |
| UA (1) | UA6023A1 (da) |
| WO (1) | WO1987002673A2 (da) |
| YU (1) | YU47185B (da) |
| ZA (1) | ZA868012B (da) |
Families Citing this family (43)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4766205A (en) * | 1985-11-13 | 1988-08-23 | Beatrice Companies, Inc. | Method for isolation of recombinant polypeptides in biologically active forms |
| JP2581668B2 (ja) * | 1985-11-27 | 1997-02-12 | 三井東圧化学株式会社 | ヒト正常細胞由来のヒト組織プラスミノ−ゲン活性化因子をコ−ドする新しいｄｎａ配列とそれを含むベクタ−及び細胞 |
| US4777043A (en) * | 1985-12-17 | 1988-10-11 | Genentech, Inc. | Stabilized human tissue plasminogen activator compositions |
| WO1988008428A1 (en) * | 1987-04-28 | 1988-11-03 | Amgen Inc. | Method for purifying granulocyte/macrophage colony stimulating factor |
| DE3722082A1 (de) * | 1987-07-03 | 1989-01-12 | Behringwerke Ag | Verfahren zur bestimmung der aktivitaet von serinproteasen oder serinproteaseinhibitoren |
| CA1340586C (en) * | 1988-09-23 | 1999-06-08 | Cetus Corporation | Process for recovering microbially produced interferon-beta |
| DE3832898A1 (de) * | 1988-09-28 | 1990-04-12 | Boehringer Mannheim Gmbh | Praeparat von in prokaryonten exprimiertem plasminogenaktivator |
| DE3835350A1 (de) * | 1988-10-17 | 1990-04-19 | Boehringer Mannheim Gmbh | Aktivierung von gentechnologisch hergestellten, in prokaryonten exprimierten antikoerpern |
| DE3903581A1 (de) * | 1989-02-07 | 1990-08-16 | Boehringer Mannheim Gmbh | Gewebs-plasminogenaktivator-derivat |
| DE3942143A1 (de) * | 1989-12-20 | 1991-06-27 | Boehringer Mannheim Gmbh | T-pa pro stabilisierung |
| JPH06500084A (ja) * | 1990-08-20 | 1994-01-06 | ノボ ノルディスク アクティーゼルスカブ | 生物学的に活性な化合物、その製造方法及びその利用 |
| EP0547102B1 (en) * | 1990-09-05 | 1998-07-08 | Southern Cross Biotech Pty.Ltd. | Solubilization of proteins in active forms |
| DE4037196A1 (de) * | 1990-11-22 | 1992-05-27 | Boehringer Mannheim Gmbh | Verfahren zur reaktivierung von denaturiertem protein |
| DE4113750A1 (de) | 1991-04-26 | 1992-10-29 | Boehringer Mannheim Gmbh | Verbesserung der renaturierung bei der sekretion von disulfidverbrueckten proteinen |
| DE4139000A1 (de) | 1991-11-27 | 1993-06-03 | Boehringer Mannheim Gmbh | Verfahren zur gentechnologischen herstellung von biologisch aktivem ss-ngf |
| US5212091A (en) * | 1992-03-02 | 1993-05-18 | Monsanto Company | Method of producing tissue factor pathway inhibitor |
| CA2109820A1 (en) * | 1992-03-24 | 1993-09-30 | George N. Cox | Refolding and purification of insulin-like growth factor i |
| EP0600372B1 (de) | 1992-12-02 | 1997-02-05 | Hoechst Aktiengesellschaft | Verfahren zur Gewinnung von Proinsulin mit korrekt verbundenen Cystinbrücken |
| DE4405179A1 (de) * | 1994-02-18 | 1995-08-24 | Hoechst Ag | Verfahren zur Gewinnung von Insulin mit korrekt verbundenen Cystinbrücken |
| FR2729972B1 (fr) * | 1995-01-31 | 1997-04-18 | Sanofi Sa | Procede d'extraction de proteines periplasmiques de microorganismes procaryotes en presence d'arginine |
| US5714371A (en) * | 1995-05-12 | 1998-02-03 | Schering Corporation | Method for refolding insoluble aggregates of hepatitis C virus protease |
| US5728804A (en) * | 1995-06-02 | 1998-03-17 | Research Corporation Technologies, Inc. | Use of cyclodextrins for protein renaturation |
| KR100305341B1 (ko) * | 1996-06-11 | 2002-03-02 | 로셰 디아그노스틱스 게엠베하 | 변성된단백질의활성화방법 |
| US7153943B2 (en) | 1997-07-14 | 2006-12-26 | Bolder Biotechnology, Inc. | Derivatives of growth hormone and related proteins, and methods of use thereof |
| US6653098B1 (en) | 1998-02-23 | 2003-11-25 | G. D. Searle & Co. | Method of producing mouse and human endostatin |
| DE19850429A1 (de) * | 1998-10-27 | 2000-05-04 | Andre Schrattenholz | Fragmente |
| EP1048732A1 (de) * | 1999-04-26 | 2000-11-02 | F. Hoffmann-La Roche Ag | Verfahren zur Herstellung von natürlich gefalteten und sekretierten Proteinen |
| EP1077263A1 (de) * | 1999-07-29 | 2001-02-21 | F.Hoffmann-La Roche Ag | Verfahren zur Herstellung von natürlich gefalteten und sekretierten Proteinen durch Co-Sekretion von Chaperonen |
| JP4873818B2 (ja) | 2000-05-16 | 2012-02-08 | ボルダー バイオテクノロジー， インコーポレイテッド | 遊離システイン残基を含有するタンパク質をリフォールディングする方法 |
| DE10105912A1 (de) * | 2001-02-09 | 2002-08-14 | Roche Diagnostics Gmbh | Rekombinante Proteinase K |
| DE10105911A1 (de) | 2001-02-09 | 2002-08-14 | Roche Diagnostics Gmbh | Expression der rekombinanten Proteinase K aus Tritirachium album in Hefe |
| DE102005033250A1 (de) | 2005-07-15 | 2007-01-18 | Bioceuticals Arzneimittel Ag | Verfahren zur Reinigung von G-CSF |
| DE202006020194U1 (de) | 2006-03-01 | 2007-12-06 | Bioceuticals Arzneimittel Ag | G-CSF-Flüssigformulierung |
| CN101506222B (zh) | 2006-07-14 | 2013-10-02 | 健泰科生物技术公司 | 重组蛋白的重折叠 |
| WO2008076933A2 (en) | 2006-12-14 | 2008-06-26 | Bolder Biotechnology, Inc. | Long acting proteins and peptides and methods of making and using the same |
| NZ601759A (en) | 2010-03-17 | 2013-07-26 | Biogenerix Gmbh | Method for obtaining biologically active recombinant human g-csf |
| AU2011317021B2 (en) * | 2010-10-20 | 2015-07-09 | Medimmune, Llc | Methods for processing inclusion bodies |
| HUP1200172A2 (en) | 2012-03-19 | 2013-10-28 | Richter Gedeon Nyrt | Methods for refolding g-csf from inclusion bodies |
| HUP1200171A1 (hu) | 2012-03-19 | 2013-09-30 | Richter Gedeon Nyrt | Módszerek polipeptidek elõállítására |
| CN103852527B (zh) * | 2012-12-05 | 2015-05-13 | 中国科学院大连化学物理研究所 | 一种高通量蛋白质样品预处理装置 |
| US10457716B2 (en) | 2014-08-06 | 2019-10-29 | University Of Notre Dame Du Lac | Protein folding and methods of using same |
| CA3044371C (en) | 2016-12-30 | 2024-01-16 | Biogend Therapeutics Co., Ltd. | Recombinant polypeptides and nucleic acid molecules, compositions, and methods of making and uses thereof |
| HRP20251064T1 (hr) | 2020-12-18 | 2025-11-07 | Richter Gedeon Nyrt. | Metode za pročišćavanje ponovno savijenog fc-peptidnog fuzionog proteina |
Family Cites Families (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4468633A (en) | 1982-04-28 | 1984-08-28 | The Bendix Corporation | Adjustable microwave power combiner for a plurality of coaxially mounted impatt diodes |
| IL68561A (en) | 1982-05-05 | 1991-01-31 | Genentech Inc | Preparation of polypeptide with human tissue plasminogen activator function,processes for making it,and dna and transformed cell intermediates thereof |
| US4432895A (en) * | 1982-11-24 | 1984-02-21 | Hoffmann-La Roche Inc. | Monomeric interferons |
| GR79124B (da) * | 1982-12-22 | 1984-10-02 | Genentech Inc | |
| JPH06102034B2 (ja) * | 1983-03-25 | 1994-12-14 | セルテク リミテツド | タンパク質の生産方法 |
| US4530787A (en) * | 1984-03-28 | 1985-07-23 | Cetus Corporation | Controlled oxidation of microbially produced cysteine-containing proteins |
| US4748234A (en) * | 1985-06-26 | 1988-05-31 | Cetus Corporation | Process for recovering refractile bodies containing heterologous proteins from microbial hosts |
| US4766205A (en) * | 1985-11-13 | 1988-08-23 | Beatrice Companies, Inc. | Method for isolation of recombinant polypeptides in biologically active forms |
| FR2596360B1 (fr) * | 1986-04-01 | 1989-02-17 | Sotralentz Sa | Conteneur sur palette avec dispositif de protection en treillis plie et renforce |
| JPH0651119A (ja) * | 1992-07-28 | 1994-02-25 | Sekisui Chem Co Ltd | 位相差板の製造方法 |
-
1985
- 1985-10-23 DE DE19853537708 patent/DE3537708A1/de active Granted
-
1986
- 1986-10-10 IE IE268386A patent/IE62634B1/en not_active IP Right Cessation
- 1986-10-15 IL IL80325A patent/IL80325A/xx not_active IP Right Cessation
- 1986-10-17 SK SK7526-86A patent/SK752686A3/sk unknown
- 1986-10-17 CZ CS867526A patent/CZ280727B6/cs not_active IP Right Cessation
- 1986-10-21 SI SI8611796A patent/SI8611796B/sl unknown
- 1986-10-21 YU YU179686A patent/YU47185B/sh unknown
- 1986-10-22 DD DD29546886A patent/DD260517A5/de not_active IP Right Cessation
- 1986-10-22 CA CA000521121A patent/CA1329157C/en not_active Expired - Lifetime
- 1986-10-22 ZA ZA868012A patent/ZA868012B/xx unknown
- 1986-10-23 UA UA4202987A patent/UA6023A1/uk unknown
- 1986-10-23 ES ES90109721T patent/ES2020498T3/es not_active Expired - Lifetime
- 1986-10-23 KR KR1019870700536A patent/KR900009139B1/ko not_active Expired
- 1986-10-23 EP EP86114731A patent/EP0219874B1/de not_active Expired - Lifetime
- 1986-10-23 HU HU865290A patent/HU204855B/hu unknown
- 1986-10-23 EP EP90109721A patent/EP0393725B1/de not_active Expired - Lifetime
- 1986-10-23 AT AT90109721T patent/ATE131489T1/de not_active IP Right Cessation
- 1986-10-23 PT PT83609A patent/PT83609B/pt not_active IP Right Cessation
- 1986-10-23 WO PCT/EP1986/000610 patent/WO1987002673A2/de not_active Ceased
- 1986-10-23 JP JP61505882A patent/JPH0728745B2/ja not_active Expired - Lifetime
- 1986-10-23 HU HU865290A patent/HUT43643A/hu unknown
- 1986-10-23 DE DE86114731T patent/DE3689404D1/de not_active Expired - Lifetime
- 1986-10-23 AU AU65993/86A patent/AU590029B2/en not_active Ceased
- 1986-10-23 DE DE3650449T patent/DE3650449D1/de not_active Expired - Lifetime
- 1986-10-23 AT AT86114731T patent/ATE98648T1/de not_active IP Right Cessation
- 1986-10-23 ES ES86114731T patent/ES2061434T3/es not_active Expired - Lifetime
- 1986-10-23 EP EP86906320A patent/EP0253823A1/de active Pending
-
1987
- 1987-06-22 SU SU874202987Q patent/SU1607689A3/ru active
- 1987-06-22 FI FI872753A patent/FI94050C/fi not_active IP Right Cessation
- 1987-06-23 DK DK198703203A patent/DK175091B1/da not_active IP Right Cessation
-
1989
- 1989-09-13 AU AU41321/89A patent/AU607083B2/en not_active Expired
-
1991
- 1991-04-12 JP JP3079762A patent/JPH0824594B2/ja not_active Expired - Lifetime
-
1992
- 1992-08-31 GR GR92300062T patent/GR920300062T1/el unknown
- 1992-10-16 HR HRP-1796/86A patent/HRP921075B1/xx not_active IP Right Cessation
-
1993
- 1993-09-03 FI FI933868A patent/FI95578C/fi not_active IP Right Cessation
-
1995
- 1995-12-14 GR GR950403376T patent/GR3018410T3/el unknown
-
1996
- 1996-08-08 HK HK153496A patent/HK153496A/xx not_active IP Right Cessation
- 1996-08-08 HK HK153596A patent/HK153596A/xx not_active IP Right Cessation
-
2000
- 2000-12-18 DK DK200001897A patent/DK175109B1/da not_active IP Right Cessation
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| DK200001897A (da) | Fremgangsmåde til aktivering af genteknologisk fremstillede, heterologe, disulfidbroer indeholdende eukaryotiske proteiner | |
| KR900006515A (ko) | 유전자 공학적으로 생성되고 원핵생물내 발현된 항체의 활성화 방법 | |
| DE69934585D1 (de) | Rückfaltung von protein-aggregaten und einschlussteilchen durch hohen druck | |
| AU2002340510A1 (en) | Process for renaturation of recombinant, disulfide containing proteins at high protein concentrations in the presence of amines | |
| EP0804461A1 (en) | Process for folding of proteins like recombinant hirudin or epidermal growth factor | |
| CZ280848B6 (cs) | Způsob aktivace genetickou technologií získaných heterologních bílkovin s obsahem disulfidových můstků eukaryotického původu po expresi v prokaryotických organismech | |
| MXPA97000658A (en) | Process for the folding of proteins as recombinant hirudine or growth factor epiderm | |
| EP1628997A2 (en) | Oxidation of peptides |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PUP | Patent expired |