NO300067B1 - Fremgangsmåte for å tilveiebringe renset, biologisk aktiv CSF-1 dimer - Google Patents
Fremgangsmåte for å tilveiebringe renset, biologisk aktiv CSF-1 dimer Download PDFInfo
- Publication number
- NO300067B1 NO300067B1 NO885555A NO885555A NO300067B1 NO 300067 B1 NO300067 B1 NO 300067B1 NO 885555 A NO885555 A NO 885555A NO 885555 A NO885555 A NO 885555A NO 300067 B1 NO300067 B1 NO 300067B1
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- Prior art keywords
- csf
- protein
- refolding
- lcsf
- dimer
- Prior art date
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- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 210000003714 granulocyte Anatomy 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 239000000710 homodimer Substances 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000012051 hydrophobic carrier Substances 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 238000005462 in vivo assay Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 1
- 229910000359 iron(II) sulfate Inorganic materials 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 210000005265 lung cell Anatomy 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- 208000008443 pancreatic carcinoma Diseases 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 101150019841 penP gene Proteins 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 1
- 101150009573 phoA gene Proteins 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 230000003134 recirculating effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 150000003355 serines Chemical class 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 238000007086 side reaction Methods 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 238000004611 spectroscopical analysis Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000012289 standard assay Methods 0.000 description 1
- 125000000446 sulfanediyl group Chemical group *S* 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 125000003831 tetrazolyl group Chemical group 0.000 description 1
- KYMBYSLLVAOCFI-UHFFFAOYSA-N thiamine Chemical compound CC1=C(CCO)SCN1CC1=CN=C(C)N=C1N KYMBYSLLVAOCFI-UHFFFAOYSA-N 0.000 description 1
- 229960003495 thiamine Drugs 0.000 description 1
- 108060008226 thioredoxin Proteins 0.000 description 1
- 229940094937 thioredoxin Drugs 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- 239000008215 water for injection Substances 0.000 description 1
- NWONKYPBYAMBJT-UHFFFAOYSA-L zinc sulfate Chemical compound [Zn+2].[O-]S([O-])(=O)=O NWONKYPBYAMBJT-UHFFFAOYSA-L 0.000 description 1
- 229910000368 zinc sulfate Inorganic materials 0.000 description 1
- 239000011686 zinc sulphate Substances 0.000 description 1
- 235000009529 zinc sulphate Nutrition 0.000 description 1
Classifications
-
- 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
- C07K14/53—Colony-stimulating factor [CSF]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- General Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Toxicology (AREA)
- Zoology (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)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Nitrogen And Oxygen Or Sulfur-Condensed Heterocyclic Ring Systems (AREA)
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US4017487A | 1987-04-16 | 1987-04-16 | |
US11400187A | 1987-10-27 | 1987-10-27 | |
PCT/US1988/001189 WO1988008003A1 (fr) | 1987-04-16 | 1988-04-18 | Production de csf-1 humain recombinant produit par des cellules bacteriennes, biologiquement actif, purifie |
Publications (3)
Publication Number | Publication Date |
---|---|
NO885555D0 NO885555D0 (no) | 1988-12-14 |
NO885555L NO885555L (no) | 1989-01-11 |
NO300067B1 true NO300067B1 (no) | 1997-04-01 |
Family
ID=26716797
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO885555A NO300067B1 (no) | 1987-04-16 | 1988-12-14 | Fremgangsmåte for å tilveiebringe renset, biologisk aktiv CSF-1 dimer |
Country Status (10)
Country | Link |
---|---|
EP (2) | EP0818466B1 (fr) |
JP (1) | JP2656964B2 (fr) |
AT (2) | ATE301133T1 (fr) |
AU (1) | AU610182B2 (fr) |
BG (1) | BG49827A3 (fr) |
DE (2) | DE3856203T2 (fr) |
FI (1) | FI96872C (fr) |
IL (1) | IL86090A (fr) |
NO (1) | NO300067B1 (fr) |
WO (1) | WO1988008003A1 (fr) |
Families Citing this family (20)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5650297A (en) * | 1986-09-17 | 1997-07-22 | Otsuka Pharmaceutical Co., Ltd. | DNA encoding human colony-stimulating factors |
US4931543A (en) * | 1987-05-11 | 1990-06-05 | Cetus Corporation | Process for recovering microbially produced interleukin-2 |
WO1989010407A1 (fr) * | 1988-04-29 | 1989-11-02 | Genetics Institute, Inc. | M-csf dimerique homogene et formulations stables pendant le stockage |
EP0410751B1 (fr) * | 1989-07-27 | 1996-04-10 | Denki Kagaku Kogyo Kabushiki Kaisha | Gène codant pour M-CSF et systèmes recombinants pour cela |
GB8927546D0 (en) * | 1989-12-06 | 1990-02-07 | Ciba Geigy | Process for the production of biologically active tgf-beta |
EP0545999B1 (fr) * | 1990-08-20 | 1997-06-04 | Novo Nordisk A/S | Procédé de préparation d l'IGF-1 biologiquement actif à partir d'un IGF-1 ayant une extension amino-terminale |
ES2119779T3 (es) * | 1990-09-05 | 1998-10-16 | Southern Cross Biotech Pty Ltd | Solubilizacion de proteinas en formas activas. |
US5288931A (en) * | 1991-12-06 | 1994-02-22 | Genentech, Inc. | Method for refolding insoluble, misfolded insulin-like growth factor-I into an active conformation |
ATE195553T1 (de) | 1992-06-09 | 2000-09-15 | Chiron Corp | Kristallisierung von m-csf |
AU661914B2 (en) * | 1992-08-18 | 1995-08-10 | Jean-Louis Odore | Support structure for a shelter cover |
CA2144523A1 (fr) * | 1993-08-04 | 1995-02-16 | Hugo Grossenbacher | Desulfatohirudine de masse moleculaire elevee |
US5663304A (en) * | 1993-08-20 | 1997-09-02 | Genentech, Inc. | Refolding of misfolded insulin-like growth factor-I |
US5407810A (en) * | 1993-08-20 | 1995-04-18 | Genentech, Inc. | Aqueous multiple-phase isolation of polypeptide |
TW517059B (en) | 1994-07-25 | 2003-01-11 | Ciba Geigy Ag | New process for the production of biologically active protein |
FR2796071B1 (fr) * | 1999-07-08 | 2001-09-07 | Hoechst Marion Roussel Inc | Procede de purification de facteur de stimulation de colonies de granulocytes |
US6808902B1 (en) | 1999-11-12 | 2004-10-26 | Amgen Inc. | Process for correction of a disulfide misfold in IL-1Ra Fc fusion molecules |
DE102004041639A1 (de) * | 2004-08-27 | 2006-03-02 | Bioceuticals Arzneimittel Ag | Verfahren zur Gewinnung von biologisch aktivem humanen G-CSF aus Inclusion Bodies |
EP3366692A1 (fr) | 2009-06-22 | 2018-08-29 | Amgen, Inc | Repliement de protéines au moyen d' un état redox chimiquement régulé |
EP2445924B2 (fr) | 2009-06-25 | 2023-12-13 | Amgen Inc. | Procédés de purification par capture de protéines exprimées dans un système non mammifère |
DE202009019091U1 (de) | 2009-12-21 | 2016-05-23 | Agilent Technologies, Inc. - A Delaware Corporation - | Fittingelement mit frontseitiger Einlage |
Family Cites Families (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GR79124B (fr) * | 1982-12-22 | 1984-10-02 | Genentech Inc | |
WO1986004607A1 (fr) * | 1985-02-05 | 1986-08-14 | Cetus Corporation | Facteur-1 recombinant stimulant la formation de colonies |
JP2579981B2 (ja) * | 1986-05-06 | 1997-02-12 | ジェネティックス・インスチチュート・インコーポレーテッド | M―csfの生産方法 |
DK54589A (da) * | 1988-02-08 | 1989-08-09 | Otsuka Pharma Co Ltd | Humane kolonistmulerende faktorer |
-
1988
- 1988-04-15 IL IL86090A patent/IL86090A/xx not_active IP Right Cessation
- 1988-04-18 EP EP97202737A patent/EP0818466B1/fr not_active Expired - Lifetime
- 1988-04-18 JP JP63503965A patent/JP2656964B2/ja not_active Expired - Lifetime
- 1988-04-18 AU AU17124/88A patent/AU610182B2/en not_active Expired
- 1988-04-18 DE DE3856203T patent/DE3856203T2/de not_active Expired - Lifetime
- 1988-04-18 DE DE3856581T patent/DE3856581T2/de not_active Expired - Lifetime
- 1988-04-18 AT AT97202737T patent/ATE301133T1/de not_active IP Right Cessation
- 1988-04-18 AT AT88904086T patent/ATE167192T1/de not_active IP Right Cessation
- 1988-04-18 EP EP88904086A patent/EP0309569B1/fr not_active Expired - Lifetime
- 1988-04-18 WO PCT/US1988/001189 patent/WO1988008003A1/fr active IP Right Grant
- 1988-12-14 NO NO885555A patent/NO300067B1/no not_active IP Right Cessation
- 1988-12-15 FI FI885807A patent/FI96872C/fi not_active IP Right Cessation
- 1988-12-16 BG BG086469A patent/BG49827A3/xx unknown
Also Published As
Publication number | Publication date |
---|---|
IL86090A0 (en) | 1988-09-30 |
DE3856203T2 (de) | 1998-10-08 |
EP0309569B1 (fr) | 1998-06-10 |
DE3856581D1 (de) | 2005-09-29 |
JPH01503440A (ja) | 1989-11-22 |
NO885555L (no) | 1989-01-11 |
WO1988008003A1 (fr) | 1988-10-20 |
EP0818466A2 (fr) | 1998-01-14 |
FI96872B (fi) | 1996-05-31 |
FI96872C (fi) | 1996-09-10 |
AU610182B2 (en) | 1991-05-16 |
ATE167192T1 (de) | 1998-06-15 |
EP0309569A1 (fr) | 1989-04-05 |
EP0818466A3 (fr) | 1998-03-25 |
BG49827A3 (en) | 1992-02-14 |
DE3856203D1 (de) | 1998-07-16 |
FI885807A0 (fi) | 1988-12-15 |
JP2656964B2 (ja) | 1997-09-24 |
DE3856581T2 (de) | 2006-05-24 |
EP0818466B1 (fr) | 2005-08-03 |
AU1712488A (en) | 1988-11-04 |
IL86090A (en) | 1993-03-15 |
NO885555D0 (no) | 1988-12-14 |
FI885807A (fi) | 1988-12-15 |
ATE301133T1 (de) | 2005-08-15 |
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FACTOR | В10106. САШү АСТIVE RECOMBINANT HUMAN |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
MK1K | Patent expired |