SI8611796B - Postopek za aktiviranje gentehnološko pripravljenih, heterolognih, eukariontskih proteinov, ki imajo disulfidne mostove, po ekspresiji v prokariontih - Google Patents
Postopek za aktiviranje gentehnološko pripravljenih, heterolognih, eukariontskih proteinov, ki imajo disulfidne mostove, po ekspresiji v prokariontih Download PDFInfo
- Publication number
- SI8611796B SI8611796B SI8611796A SI8611796A SI8611796B SI 8611796 B SI8611796 B SI 8611796B SI 8611796 A SI8611796 A SI 8611796A SI 8611796 A SI8611796 A SI 8611796A SI 8611796 B SI8611796 B SI 8611796B
- Authority
- SI
- Slovenia
- Prior art keywords
- process according
- carried out
- concentration
- denaturing
- mol
- Prior art date
Links
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)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- General Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (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)
- Mechanical Treatment Of Semiconductor (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Lubricants (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
Claims (38)
- © · · © © © ©ο c Ο »0 0 6 Ο © © Ο © Ο 0 © ©ο © I ©Ο ©Ο© © © © CCO ο c β ο c c ο f' ο c < r. ο © η η r. r r r c r· > ' r 1 PATENTNI ZAHTEVKI 1. Postopek za aktiviranje gentehnološko pripravljenih, heterolognih, eukariontskih proteinov, ki vsebujejo disulfidne mostove, po ekspresiji v prokariontih, z a) razklopom prokariontskih celic, b) solubiliziranjem eukarionskih proteinov pri denaturirnih in reducirnih pogojih, c) odločenjem redukcijskih/denaturirnih sredstev, d) reaktiviranjem pri oksidirnih pogojih s e) prevedbo tiolnih skupin solubiliziranih proteinov v mešane disulfide proteina in glutationa ob dodatku GSSG pri denaturirnih pogojih, f) tvorbo aktivnega proteina iz mešanih disulfidov pri koncentraciji GSH 0,5 do 5 mmol/1, pri pH vrednosti 7 do 10,5 ter pri ne-denaturirni koncentraciji denaturirnega sredstva.
- 2. Postopek po zahtevku 1, označen s tem, da izvedemo ekspresijo v E. coli ali P. putida.
- 3. Postopek po zahtevku 1 ali 2, označen s tem, da v stopnji reaktiviranja uporabimo kot denaturirno sredstvo arginin, gvanidin hidroklorid in/ali vsaj eno spojino s splošno formulo R2-CO-NRR, (I), v kateri R in Rj pomenita vodik ali alkil z 1 do 4 atomi ogljika, R2 pa vodik ali NHR, ali alkil z 1 do 3 atomi ogljika.
- 4. Postopek po zahtevku 3, označen s tem, da znaša koncentracija arginina in/ali gvanidinhidroklorida 0,1 do 1,0 mol/1, zlasti 0,25 do 0,8 mol/1.
- 5. Postopek po zahtevku 3, označen s tem, da znaša koncentracija spojine s splošno formulo I 0,5 do 4 mol/1. zlasti 1 do 3,5 mol/1.
- 6. Postopek po enem izmed prejšnjih zahtevkov, označen s tem, da delamo pri stopnji reaktiviranja v prisotnosti neproteolitično učinkovitega proteina, zlasti v prisotnosti albumina iz govejega seruma.
- 7. Postopek po enem izmed prejšnjih zahtevkov, označen s tem, da izvedemo celični razklop s pomočjo ultra zvoka, visokotlačne disperzije ali lizocima.
- 8. Postopek po zahtevku 7, označen s tem, da izvedemo razklop v razredčeni vodni pufrski raztopini, zlasti v 0,1 mol/1 Tris, pri nevtralni do šibko kisli pH vrednosti. ο ο 00 00 0 ο Ο Ο (' 0 0 ο ο 00 00 0 ο Ο Ο (' 0 0© c c © ooco ο c η f' r C Ο © Ο C © crr r r r r··- crr· r f? r c r r <- r r. r, f r r r r <· > 2
- 9. Postopek po enem izmed prejšnjih zahtevkov, označen s tem, da po celičnem razklopu odločimo netopne sestavine.
- 10. Postopek po enem izmed prejšnjih zahtevkov, označen s tem, da pri stopnji solubiliziranja delamo pri alkalni pH vrednosti v prisotnosti redukcijskega sredstva iz merkapto skupine ter v prisotnosti denaturirnega sredstva.
- 11. Postopek po zahtevku 10, označen s tem, da delamo v prisotnosti gvanidinhidrok-lorida in/ali spojine s splošno formulo I kot denaturirnega sredstva.
- 12. Postopek po zahtevku 11, označen s tem, da znaša koncentracija gvanidinhidrok-lorida 6 mol/1, koncentracija spojine s splošno formulo I pa 8 mol/1.
- 13. Postopek po enem izmed zahtevkov 10 do 12, označen s tem, da delamo v prisotnosti DTE, /3-merkaptoetanola, cisteina ali GSH.
- 14. Postopek po enem izmed prejšnjih zahtevkov, označen s tem, da izvedemo čiščenje in odločenje redukcijskih, oksidacijskih ali denaturirnih sredstev s pomočjo sterične izločevalne kromatografije ali dialize.
- 15. Postopek po enem izmed prejšnjih zahtevkov, označen s tem, da po stopnji reak-tiviranja izvedemo čistilno stopnjo s pomočjo dialize.
- 16. Postopek po enem izmed zahtevkov 1 do 15, označen s tem, da kot gentehnološko pripravljen eukariontski protein uporabimo t-PA.
- 17. Stimuliranja sposoben neglikoziliran tPA, ki se ga da dobiti po postopku po enem izmed zahtevkov 1 do 16.
- 18. Postopek po zahtevku 6, označen s tem, da odločimo mešani disulfid proteina in glutationa z ionsko izmenjevalno obdelavo od nemodificiranega proteina.
- 19. Postopek za aktiviranje gentehnološko prirpavljenih, heterolognih, eukariontskih proteinov, ki vsebujejo disulfidne mostove, po ekspresiji v prokariontih s celičnim razklopom, solubiliziranjem ob denaturirnih in reducirnih pogojih ter reaktivirajem ob oksidirnih pogojih v prisotnosti GSH/GSSG, označen s tem, da pri stopnji reak- ©Ο ©Ο Ο© ©© f> © ¢-,0 0 0eecc r e e © c r o r c c © c r r © en r c- r c c- c r < r r f r- r r·- ' * c «· r r , , 3 tiviranja delamo s pH vrednostjo 8 do 12, koncentracijo GSH 0,1 do 20 mmol/1, koncentracijo GSSG 0,01 do 3 mmol/1 ter ne-denaturirno koncentracijo denaturirnega sredstva ter da v stopnji reaktiviranja uporabimo kot denaturirno sredstvo arginin in/ali vsaj eno spojino s splošno formulo R2-CO-NRRj (I), v kateri R in Rj pomenita vodik ali alkil z 1 do 4 atomi ogljika, R2 pa vodik ali NHR( ali alkil z 1 do 3 atomi ogljika, pod pogojem, da R in R, nista istočasno vodik.
- 20. Postopek po zahtevku 19, označen s tem, da v stopnji reaktiviranja znaša pH vrednost 9,5 do 11.
- 21. Postopek po enem izmed zahtevkov 19 in 20, označen s tem, da v stopnji rak-tiviranja znaša koncentracija GSH 0,2 do 10 mmol/1 in/ali koncentracija GSSG 0,05 do 1 mmol/1.
- 22. Postopek po enem izmed zahtevkov 19-21, označen s tem, da po solubiliziranju in pred reaktiviranjem izvedemo stopnjo čiščenja.
- 23. Postopek po enem izmed zahtevkov 19-21, označen s tein, da izvedemo reak-tiviranje brez predhodnega odločenja denaturirno/redukcijskega sredstva, pri čemer reakcijsko raztopino po denaturiranju/redukciji razredčimo z reaktivirnim pufrom ter pri naslednjem reaktiviranju koncentracija GSSG prekorači preostalo rezidualno koncentracijo DTE.
- 24. Postopek po enem izmed zahtevkov 19-23, označen s tem, da izvedemo ekspresijo v E. coli ali P.putida.
- 25. Postopek po enem izmed zahtevkov 19-24, označen s tem, da znaša koncentracija arginina 0,1 do 1,0 mol/1, zlasti 0,25 do 0,8 mol/1.
- 26. Postopek po enem od zahtevkov 19-24, označen s tem, da znaša koncentracija spojine s splošno formulo I 0,5 do 4 mol/1, zlasti 1 do 3,5 mol/1.
- 27. Postopek po enem izmed zahtevkov 19-26, označen s tem, da delamo pri stopnji reaktiviranja v prisotnosti neproteolitično učinkovitega proteina, zlasti v prisotnosti albumina iz govejega seruma.
- 28. Postopek po enem izmed zahtevkov 19-27, označen s tem, da izvedemo celični ο© ©O ·© ©© ©ο ο·ΦΟ OCOO © Ο © © ©ο Ο©Ο © Ο Φ Ο c © ©ο© ο © c η ο ο © οο ^ Λ r r ο Ο C '· © r> r r ¢: 4 razklop s pomočjo ultra zvoka, visokotlačne disperzije ali lizocima.
- 29. Postopek po zahtevku 28, označen s tem, da izvedemo razklop v razredčeni vodni pufrski raztopini, zlasti v 0,1 mol/l Tris, pri nevtralni do šibko kisli pH vrednosti.
- 30. Postopek po enem izmed zahtevkov 19-29, označen s tem, da po celičnem razklopu odločimo netopne sestavine.
- 31. Postopek po enem izmed zahtevkov 19-30, označen s tem, da pri stopnji solubiliziranja delamo pri alkalni pH vrednosti v prisotnosti redukcijskega sredstva iz merkapto skupine ter v prisotnosti denaturirnega sredstva.
- 32. Postopek po zahtevku 31, označen s tem, da delamo v prisotnosti spojine s splošno formulo I kot denaturirnega sredstva.
- 33. Postopek po zahtevku 32, označen s tem, da znaša koncentracija spojine s splošno formulo Ϊ 8 mol/l.
- 34. Postopek po enem izmed zahtevkov 31 do 33, označen s tem, da delamo v prisotnosti DTE, /3-merkaptoetanola, cisteina ali GSH.
- 35. Postopek po enem izmed zahtevkov 19-34, označen s tem, da izvedemo čiščenje in odločenje redukcijskih, oksidacijskih ali denaturirnih sredstev s pomočjo sterične izločevalne kromatografije ali dialize.
- 36. Postopek po enem izmed zahtevkov 19-35, označen s tem, da po stopnji reak-tiviranja izvedemo čistilno stopnjo s pomočjo dialize.
- 37. Postopek po enem izmed zahtevkov 19-36, označen s tem, da kot gentehnološko pripravljen eukariontski protein uporabimo t-PA.
- 38. Postopek po enem izmed zahtevkov 19-36, označen s tem, da kot gentehnološko pripravljen eukariontski protein uporabimo inteferon-/3.
Applications Claiming Priority (2)
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 |
YU179686A YU47185B (sh) | 1985-10-23 | 1986-10-21 | Postupak za aktiviranje heterolognih eukariotskih proteina, pripremljenih gen-tehnologijom koji imaju disulfidne mostove polse ekspresije u prokariotima |
Publications (2)
Publication Number | Publication Date |
---|---|
SI8611796A SI8611796A (sl) | 1996-10-31 |
SI8611796B true SI8611796B (sl) | 1998-06-30 |
Family
ID=6284269
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
SI8611796A SI8611796B (sl) | 1985-10-23 | 1986-10-21 | Postopek za aktiviranje gentehnološko pripravljenih, heterolognih, eukariontskih proteinov, ki imajo disulfidne mostove, po ekspresiji v prokariontih |
Country Status (26)
Country | Link |
---|---|
EP (3) | EP0219874B1 (sl) |
JP (2) | JPH0728745B2 (sl) |
KR (1) | KR900009139B1 (sl) |
AT (2) | ATE131489T1 (sl) |
AU (2) | AU590029B2 (sl) |
CA (1) | CA1329157C (sl) |
CZ (1) | CZ280727B6 (sl) |
DD (1) | DD260517A5 (sl) |
DE (3) | DE3537708A1 (sl) |
DK (2) | DK175091B1 (sl) |
ES (2) | ES2020498T3 (sl) |
FI (2) | FI94050C (sl) |
GR (2) | GR920300062T1 (sl) |
HK (2) | HK153496A (sl) |
HR (1) | HRP921075B1 (sl) |
HU (2) | HUT43643A (sl) |
IE (1) | IE62634B1 (sl) |
IL (1) | IL80325A (sl) |
PT (1) | PT83609B (sl) |
SI (1) | SI8611796B (sl) |
SK (1) | SK278317B6 (sl) |
SU (1) | SU1607689A3 (sl) |
UA (1) | UA6023A1 (sl) |
WO (1) | WO1987002673A2 (sl) |
YU (1) | YU47185B (sl) |
ZA (1) | ZA868012B (sl) |
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 |
AU621051B2 (en) | 1987-04-28 | 1992-03-05 | 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 |
ATE154073T1 (de) * | 1990-08-20 | 1997-06-15 | Novo Nordisk As | Prozess für die herstellung von biologisch aktivem igf-1 durch verwendung von amino-terminal verlängertem igf-1 |
DE69129747T2 (de) * | 1990-09-05 | 1998-11-12 | Southern Cross Biotech Pty Ltd | In lösung bringen von proteinen in aktiver form |
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 |
WO1993019084A1 (en) * | 1992-03-24 | 1993-09-30 | Synergen, Inc. | 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 |
CA2257122C (en) * | 1996-06-11 | 2004-04-06 | Boehringer Mannheim Gmbh | Method of activating denatured protein |
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 |
DE60129432T2 (de) | 2000-05-16 | 2008-04-17 | Bolder Biotechnology, Inc., Louisville | Verfahren zur rückfaltung von proteinen mit freien cysteinresten |
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 |
WO2008008975A2 (en) | 2006-07-14 | 2008-01-17 | Genentech, Inc. | Refolding of recombinant proteins |
EP2102355B1 (en) | 2006-12-14 | 2016-03-02 | Bolder Biotechnology, Inc. | Long acting proteins and peptides and methods of making and using the same |
AU2011229491B2 (en) | 2010-03-17 | 2015-02-05 | Ratiopharm Gmbh | Method for obtaining biologically active recombinant human G-CSF |
WO2012054679A1 (en) * | 2010-10-20 | 2012-04-26 | Medimmune, Llc | Methods for processing inclusion bodies |
HUP1200171A1 (hu) | 2012-03-19 | 2013-09-30 | Richter Gedeon Nyrt | Módszerek polipeptidek elõállítására |
HUP1200172A2 (en) | 2012-03-19 | 2013-10-28 | Richter Gedeon Nyrt | Methods for refolding g-csf from inclusion bodies |
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 |
NZ746109A (en) | 2016-12-30 | 2022-12-23 | Biogend Therapeutics Co Ltd | Recombinant polypeptides and nucleic acid molecules, compositions, and methods of making and uses thereof |
WO2022129460A1 (en) | 2020-12-18 | 2022-06-23 | Richter Gedeon Nyrt. | Methods for the purification of refolded fc-peptide fusion protein |
Family Cites Families (12)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS5135481A (ja) * | 1974-09-18 | 1976-03-25 | Fujiwa Kako Kk | Kojundohitorokinaaze no seiho |
US4468633A (en) | 1982-04-28 | 1984-08-28 | The Bendix Corporation | Adjustable microwave power combiner for a plurality of coaxially mounted impatt diodes |
AR241654A1 (es) | 1982-05-05 | 1992-10-30 | Genentech Inc | Procedimiento para producir activador de plasminogeno de tejido humano. |
US4432895A (en) * | 1982-11-24 | 1984-02-21 | Hoffmann-La Roche Inc. | Monomeric interferons |
GR79124B (sl) * | 1982-12-22 | 1984-10-02 | Genentech Inc | |
WO1984003711A1 (en) * | 1983-03-25 | 1984-09-27 | Celltech Ltd | A process for the production of a protein |
JPS6051119A (ja) * | 1983-08-30 | 1985-03-22 | Green Cross Corp:The | ウロキナ−ゼ乾燥製剤 |
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 CZ CS867526A patent/CZ280727B6/cs not_active IP Right Cessation
- 1986-10-17 SK SK7526-86A patent/SK278317B6/sk unknown
- 1986-10-21 YU YU179686A patent/YU47185B/sh unknown
- 1986-10-21 SI SI8611796A patent/SI8611796B/sl unknown
- 1986-10-22 ZA ZA868012A patent/ZA868012B/xx 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
- 1986-10-23 ES ES90109721T patent/ES2020498T3/es not_active Expired - Lifetime
- 1986-10-23 JP JP61505882A patent/JPH0728745B2/ja not_active Expired - Lifetime
- 1986-10-23 UA UA4202987A patent/UA6023A1/uk unknown
- 1986-10-23 AT AT90109721T patent/ATE131489T1/de not_active IP Right Cessation
- 1986-10-23 WO PCT/EP1986/000610 patent/WO1987002673A2/de active IP Right Grant
- 1986-10-23 HU HU865290A patent/HUT43643A/hu unknown
- 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 AU AU65993/86A patent/AU590029B2/en not_active Ceased
- 1986-10-23 EP EP86114731A patent/EP0219874B1/de not_active Expired - Lifetime
- 1986-10-23 DE DE3650449T patent/DE3650449D1/de not_active Expired - Lifetime
- 1986-10-23 EP EP90109721A patent/EP0393725B1/de not_active Expired - Lifetime
- 1986-10-23 PT PT83609A patent/PT83609B/pt not_active IP Right Cessation
- 1986-10-23 EP EP86906320A patent/EP0253823A1/de active Pending
- 1986-10-23 DE DE86114731T patent/DE3689404D1/de not_active Expired - Lifetime
- 1986-10-23 HU HU865290A patent/HU204855B/hu unknown
- 1986-10-23 KR KR1019870700536A patent/KR900009139B1/ko not_active IP Right Cessation
-
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 |
---|---|---|
SI8611796B (sl) | Postopek za aktiviranje gentehnološko pripravljenih, heterolognih, eukariontskih proteinov, ki imajo disulfidne mostove, po ekspresiji v prokariontih | |
Fischer et al. | Isolation, renaturation, and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies | |
EP0400472B1 (en) | Process for preparing polyethylene glycol derivatives and modified protein. | |
KR900006515A (ko) | 유전자 공학적으로 생성되고 원핵생물내 발현된 항체의 활성화 방법 | |
AU618386B2 (en) | Method for naturation of somatotropin protein | |
KITAGAWA et al. | Amino Acid Sequence of Copper, Zinc-Superoxide Dimutase from Spinach Leaves | |
Dixon et al. | Conversion of the N-terminal serine residue of corticotrophin into glycine | |
JP3047923B2 (ja) | ケラチン有機溶媒液およびその製造法 | |
JPH01132598A (ja) | 変性剤溶液中に含まれる組換え蛋白質における分子内ジスルフィド結合の生成を促進する方法 | |
AU664021B2 (en) | Solubilization of proteins in active forms | |
EP1095055B1 (en) | Method for the production of recombinant peptides with a low amount of trisulfides | |
EP0263902B1 (en) | Solubilisation and oxidation of somatotropin from transformed microorganisms | |
Pieniaźek et al. | The participation of methionine and cysteine in the formation of bonds resistant to the action of proteolytic enzymes in heated casein | |
BÜLLESBACH et al. | Human Proinsulin, VIII. Studies on the S-Tritylation of Reduced Proinsulin, Insulin A and B Chains and their Detritylation | |
EP0347105B1 (en) | S-sulfonated calcitonin derivatives | |
PAYNOVICH et al. | OXIDATION OF THE SULFHYDRYL FORMS OF INSULIN A‐CHAIN AND B‐CHAIN | |
JP6289937B2 (ja) | リラキシンの製造方法 | |
KR20050058243A (ko) | 아민의 존재하에서 높은 단백질 농도에서 이황화물-함유재조합 단백질을 탈변성하는 방법 | |
Lazure et al. | The ostrich pituitary contains a major peptide homologous to mammalian chromogranin A (1–76) | |
IE66142B1 (en) | Method for solubilization and naturation of somatotropins utilzing low area concentration | |
KR20000017601A (ko) | 봉입체 형태의 소마토트로핀을 활성 형태로 제조하는 방법 | |
WO1996003425A1 (en) | Process for folding of proteins like recombinant hirudin or epidermal growth factor | |
Boon et al. | Protection and deprotection of horse cytochrome c | |
JP5726436B2 (ja) | 変性ペプチドの製造方法及び変性ペプチド | |
US20070042460A1 (en) | Oxidation of peptides |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
IF | Valid on the event date |