JP4019432B2 - ヒトアクチビンａのリフォールディング方法 - Google Patents
ヒトアクチビンａのリフォールディング方法 Download PDFInfo
- Publication number
- JP4019432B2 JP4019432B2 JP52349797A JP52349797A JP4019432B2 JP 4019432 B2 JP4019432 B2 JP 4019432B2 JP 52349797 A JP52349797 A JP 52349797A JP 52349797 A JP52349797 A JP 52349797A JP 4019432 B2 JP4019432 B2 JP 4019432B2
- Authority
- JP
- Japan
- Prior art keywords
- human activin
- refolding
- buffer
- biological activity
- activin
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 108010023082 activin A Proteins 0.000 title claims description 116
- 238000000034 method Methods 0.000 title claims description 29
- 239000000872 buffer Substances 0.000 claims description 74
- 125000003396 thiol group Chemical group [H]S* 0.000 claims description 26
- 230000004071 biological effect Effects 0.000 claims description 23
- 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 claims description 22
- GEHJYWRUCIMESM-UHFFFAOYSA-L sodium sulfite Chemical compound [Na+].[Na+].[O-]S([O-])=O GEHJYWRUCIMESM-UHFFFAOYSA-L 0.000 claims description 20
- AWDRATDZQPNJFN-VAYUFCLWSA-N taurodeoxycholic 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)NCCS(O)(=O)=O)C)[C@@]2(C)[C@@H](O)C1 AWDRATDZQPNJFN-VAYUFCLWSA-N 0.000 claims description 19
- 108010024636 Glutathione Proteins 0.000 claims description 13
- -1 thiol compound Chemical class 0.000 claims description 12
- 238000006243 chemical reaction Methods 0.000 claims description 10
- 235000010265 sodium sulphite Nutrition 0.000 claims description 10
- 229960003180 glutathione Drugs 0.000 claims description 8
- 239000000126 substance Substances 0.000 claims description 7
- 230000003139 buffering effect Effects 0.000 claims description 6
- 230000002829 reductive effect Effects 0.000 claims description 6
- 150000003839 salts Chemical class 0.000 claims description 4
- 238000004925 denaturation Methods 0.000 claims description 3
- 230000036425 denaturation Effects 0.000 claims description 3
- 230000000694 effects Effects 0.000 claims description 3
- 230000008569 process Effects 0.000 claims description 3
- 239000004475 Arginine Substances 0.000 claims 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims 1
- 238000012216 screening Methods 0.000 claims 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 46
- 239000007983 Tris buffer Substances 0.000 description 44
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 44
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 31
- 239000004202 carbamide Substances 0.000 description 31
- BHTRKEVKTKCXOH-UHFFFAOYSA-N Taurochenodesoxycholsaeure Natural products OC1CC2CC(O)CCC2(C)C2C1C1CCC(C(CCC(=O)NCCS(O)(=O)=O)C)C1(C)CC2 BHTRKEVKTKCXOH-UHFFFAOYSA-N 0.000 description 17
- 229950005578 tidiacic Drugs 0.000 description 17
- 239000003153 chemical reaction reagent Substances 0.000 description 16
- 239000011734 sodium Substances 0.000 description 16
- 238000004519 manufacturing process Methods 0.000 description 13
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 12
- 238000004007 reversed phase HPLC Methods 0.000 description 12
- 235000018102 proteins Nutrition 0.000 description 11
- 108090000623 proteins and genes Proteins 0.000 description 11
- 102000004169 proteins and genes Human genes 0.000 description 11
- 239000000243 solution Substances 0.000 description 10
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 9
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 9
- 229960003589 arginine hydrochloride Drugs 0.000 description 9
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 8
- 210000004027 cell Anatomy 0.000 description 8
- 229960000789 guanidine hydrochloride Drugs 0.000 description 8
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 8
- 239000012528 membrane Substances 0.000 description 8
- 244000005700 microbiome Species 0.000 description 8
- 238000001228 spectrum Methods 0.000 description 8
- 238000000502 dialysis Methods 0.000 description 7
- 208000032839 leukemia Diseases 0.000 description 7
- 238000006722 reduction reaction Methods 0.000 description 7
- 241000588724 Escherichia coli Species 0.000 description 6
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 210000004102 animal cell Anatomy 0.000 description 6
- 239000008187 granular material Substances 0.000 description 6
- 230000006872 improvement Effects 0.000 description 6
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 5
- 239000000306 component Substances 0.000 description 5
- 239000012228 culture supernatant Substances 0.000 description 5
- 230000001939 inductive effect Effects 0.000 description 5
- 238000011160 research Methods 0.000 description 5
- 238000000926 separation method Methods 0.000 description 5
- 108010053070 Glutathione Disulfide Proteins 0.000 description 4
- 150000001413 amino acids Chemical class 0.000 description 4
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 4
- 235000018417 cysteine Nutrition 0.000 description 4
- 230000004069 differentiation Effects 0.000 description 4
- 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 description 4
- 238000005259 measurement Methods 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- YPZRWBKMTBYPTK-UHFFFAOYSA-N oxidized gamma-L-glutamyl-L-cysteinylglycine Natural products OC(=O)C(N)CCC(=O)NC(C(=O)NCC(O)=O)CSSCC(C(=O)NCC(O)=O)NC(=O)CCC(N)C(O)=O YPZRWBKMTBYPTK-UHFFFAOYSA-N 0.000 description 4
- 239000002994 raw material Substances 0.000 description 4
- 238000011084 recovery Methods 0.000 description 4
- 230000004083 survival effect Effects 0.000 description 4
- UMCMPZBLKLEWAF-BCTGSCMUSA-N 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CCCS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 UMCMPZBLKLEWAF-BCTGSCMUSA-N 0.000 description 3
- 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 3
- 230000008859 change Effects 0.000 description 3
- 239000003638 chemical reducing agent Substances 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 238000009776 industrial production Methods 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
- 229940024606 amino acid Drugs 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- VSGNNIFQASZAOI-UHFFFAOYSA-L calcium acetate Chemical compound [Ca+2].CC([O-])=O.CC([O-])=O VSGNNIFQASZAOI-UHFFFAOYSA-L 0.000 description 2
- 239000001639 calcium acetate Substances 0.000 description 2
- 235000011092 calcium acetate Nutrition 0.000 description 2
- 229960005147 calcium acetate Drugs 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 239000013024 dilution buffer Substances 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 239000012091 fetal bovine serum Substances 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 239000003223 protective agent Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- HAEPBEMBOAIUPN-UHFFFAOYSA-L sodium tetrathionate Chemical compound O.O.[Na+].[Na+].[O-]S(=O)(=O)SSS([O-])(=O)=O HAEPBEMBOAIUPN-UHFFFAOYSA-L 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- XFNJVJPLKCPIBV-UHFFFAOYSA-N trimethylenediamine Chemical compound NCCCN XFNJVJPLKCPIBV-UHFFFAOYSA-N 0.000 description 2
- 102100027324 2-hydroxyacyl-CoA lyase 1 Human genes 0.000 description 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 101001009252 Homo sapiens 2-hydroxyacyl-CoA lyase 1 Proteins 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 230000000875 corresponding effect Effects 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 239000003398 denaturant Substances 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
- 150000002019 disulfides Chemical class 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 229960004198 guanidine Drugs 0.000 description 1
- 239000001307 helium Substances 0.000 description 1
- 229910052734 helium Inorganic materials 0.000 description 1
- SWQJXJOGLNCZEY-UHFFFAOYSA-N helium atom Chemical compound [He] SWQJXJOGLNCZEY-UHFFFAOYSA-N 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000011261 inert gas Substances 0.000 description 1
- 239000012533 medium component Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 208000025113 myeloid leukemia Diseases 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- PHEDXBVPIONUQT-RGYGYFBISA-N phorbol 13-acetate 12-myristate Chemical compound C([C@]1(O)C(=O)C(C)=C[C@H]1[C@@]1(O)[C@H](C)[C@H]2OC(=O)CCCCCCCCCCCCC)C(CO)=C[C@H]1[C@H]1[C@]2(OC(C)=O)C1(C)C PHEDXBVPIONUQT-RGYGYFBISA-N 0.000 description 1
- 239000002644 phorbol ester Substances 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 239000012679 serum free medium Substances 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- RPACBEVZENYWOL-XFULWGLBSA-M sodium;(2r)-2-[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylate Chemical compound [Na+].C=1C=C(Cl)C=CC=1OCCCCCC[C@]1(C(=O)[O-])CO1 RPACBEVZENYWOL-XFULWGLBSA-M 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 230000006103 sulfonylation Effects 0.000 description 1
- 238000005694 sulfonylation reaction Methods 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
Classifications
-
- 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
- C07K14/575—Hormones
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Toxicology (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Gastroenterology & Hepatology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Endocrinology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP7-333070 | 1995-12-21 | ||
| JP33307095 | 1995-12-21 | ||
| PCT/JP1996/003700 WO1997023638A1 (fr) | 1995-12-21 | 1996-12-19 | Procede pour replier l'activine a humaine |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPWO1997023638A1 JPWO1997023638A1 (ja) | 1999-01-26 |
| JP4019432B2 true JP4019432B2 (ja) | 2007-12-12 |
Family
ID=18261933
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP52349797A Expired - Lifetime JP4019432B2 (ja) | 1995-12-21 | 1996-12-19 | ヒトアクチビンａのリフォールディング方法 |
Country Status (5)
| Country | Link |
|---|---|
| US (1) | US6084076A (OSRAM) |
| EP (1) | EP0943690B1 (OSRAM) |
| JP (1) | JP4019432B2 (OSRAM) |
| DE (1) | DE69636739T2 (OSRAM) |
| WO (1) | WO1997023638A1 (OSRAM) |
Families Citing this family (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP4055248B2 (ja) | 1998-05-25 | 2008-03-05 | 味の素株式会社 | 精製ヒトアクチビン及びその製造方法 |
| US7442370B2 (en) * | 2001-02-01 | 2008-10-28 | Biogen Idec Ma Inc. | Polymer conjugates of mutated neublastin |
| US7276580B2 (en) * | 2001-03-12 | 2007-10-02 | Biogen Idec Ma Inc. | Neurotrophic factors |
| GB0220199D0 (en) * | 2002-08-30 | 2002-10-09 | Univ Utrecht | Mutant protein and refolding method |
| JP4571776B2 (ja) * | 2002-11-05 | 2010-10-27 | Ｊｘ日鉱日石エネルギー株式会社 | 潤滑油組成物 |
| WO2004056872A1 (ja) * | 2002-12-20 | 2004-07-08 | Mitsubishi Pharma Corporation | タンパク質のチオール基を保護する方法 |
| NZ543365A (en) | 2003-04-18 | 2009-02-28 | Biogen Idec Inc | Polymer-conjugated glycosylated neublastin |
| EP1786454B1 (en) * | 2004-08-19 | 2010-07-21 | Biogen Idec MA Inc. | Neublastin variants |
| DE602005022082D1 (de) * | 2004-08-19 | 2010-08-12 | Biogen Idec Inc | Rückfaltung von proteinen der transforming-growth-factor-beta-familie |
| TWI501774B (zh) * | 2006-02-27 | 2015-10-01 | Biogen Idec Inc | 神經性病症之治療 |
| ES2450065T3 (es) * | 2006-03-01 | 2014-03-21 | Biogen Idec Ma Inc. | Composiciones y métodos para la administración de proteínas de la familia de ligandos del GDNF |
| GB0604966D0 (en) | 2006-03-11 | 2006-04-19 | Renovo Ltd | Medicaments and proteins |
| GB0604938D0 (en) | 2006-03-11 | 2006-04-19 | Renovo Ltd | Proteins, nucleic acids and medicaments |
| GB0604964D0 (en) | 2006-03-11 | 2006-04-19 | Renovo Ltd | Protein folding |
| US8329655B2 (en) | 2007-05-01 | 2012-12-11 | Biogen Idec Ma Inc. | Methods for increasing vascularization |
| US20110135648A1 (en) * | 2007-08-08 | 2011-06-09 | Biogen Idec Ma Inc. | Anti-neublastin antibodies and uses thereof |
| JP2016183118A (ja) * | 2015-03-25 | 2016-10-20 | 東ソー株式会社 | 増殖因子前駆体のリフォールディング方法 |
| JP7325722B2 (ja) | 2018-03-22 | 2023-08-15 | 味の素株式会社 | 組換えアクチビンａ前駆体タンパク質 |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS63119679A (ja) * | 1985-10-03 | 1988-05-24 | ジエネンテク，インコ−ポレイテツド | インヒビンのα鎖またはβ鎖をコ−ドしている核酸、並びにその様な核酸を用いてポリペプチドを合成する方法 |
| US4798885A (en) * | 1986-02-07 | 1989-01-17 | Genentech, Inc. | Compositions of hormonally active human and porcine inhibin containing an α chain and 62 chain |
| DE3835350A1 (de) * | 1988-10-17 | 1990-04-19 | Boehringer Mannheim Gmbh | Aktivierung von gentechnologisch hergestellten, in prokaryonten exprimierten antikoerpern |
| GB8927546D0 (en) * | 1989-12-06 | 1990-02-07 | Ciba Geigy | Process for the production of biologically active tgf-beta |
| US5144006A (en) * | 1991-06-13 | 1992-09-01 | The Rockefeller University | Oxidative folding of peptide and protein substrates using hydrocarbon sulfoxides |
| US5658876A (en) * | 1994-04-28 | 1997-08-19 | The General Hospital Corporation | Activin antagonists as novel contraceptives |
| TW517059B (en) * | 1994-07-25 | 2003-01-11 | Ciba Geigy Ag | New process for the production of biologically active protein |
| TW440566B (en) * | 1994-07-25 | 2001-06-16 | Novartis Ag | Novel process for the production of biologically active dimeric protein |
-
1996
- 1996-12-19 JP JP52349797A patent/JP4019432B2/ja not_active Expired - Lifetime
- 1996-12-19 DE DE69636739T patent/DE69636739T2/de not_active Expired - Lifetime
- 1996-12-19 US US09/091,265 patent/US6084076A/en not_active Expired - Lifetime
- 1996-12-19 WO PCT/JP1996/003700 patent/WO1997023638A1/ja not_active Ceased
- 1996-12-19 EP EP96942573A patent/EP0943690B1/en not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| WO1997023638A1 (fr) | 1997-07-03 |
| EP0943690A1 (en) | 1999-09-22 |
| DE69636739T2 (de) | 2007-10-18 |
| US6084076A (en) | 2000-07-04 |
| DE69636739D1 (de) | 2007-01-11 |
| EP0943690B1 (en) | 2006-11-29 |
| EP0943690A4 (OSRAM) | 1999-09-22 |
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