DD289544A5 - Stabile bioaktive somatotropine - Google Patents
Stabile bioaktive somatotropine Download PDFInfo
- Publication number
- DD289544A5 DD289544A5 DD89332530A DD33253089A DD289544A5 DD 289544 A5 DD289544 A5 DD 289544A5 DD 89332530 A DD89332530 A DD 89332530A DD 33253089 A DD33253089 A DD 33253089A DD 289544 A5 DD289544 A5 DD 289544A5
- Authority
- DD
- German Democratic Republic
- Prior art keywords
- somatotropin
- small loop
- derivatized
- sulfhydryl groups
- loop
- Prior art date
Links
- 230000000975 bioactive effect Effects 0.000 title claims abstract description 14
- 108010051696 Growth Hormone Proteins 0.000 claims abstract description 117
- 102000018997 Growth Hormone Human genes 0.000 claims abstract description 117
- 238000000034 method Methods 0.000 claims abstract description 40
- 125000003396 thiol group Chemical group [H]S* 0.000 claims abstract description 28
- 239000000539 dimer Substances 0.000 claims abstract description 7
- -1 oligomers Substances 0.000 claims abstract description 7
- 230000008569 process Effects 0.000 claims abstract description 7
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 claims description 16
- PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical compound NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 claims description 12
- 239000003638 chemical reducing agent Substances 0.000 claims description 11
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 claims description 8
- 239000000122 growth hormone Substances 0.000 claims description 8
- 241000283690 Bos taurus Species 0.000 claims description 6
- 125000004432 carbon atom Chemical group C* 0.000 claims description 6
- 125000000217 alkyl group Chemical group 0.000 claims description 3
- DHXNZYCXMFBMHE-UHFFFAOYSA-N 3-bromopropanoic acid Chemical compound OC(=O)CCBr DHXNZYCXMFBMHE-UHFFFAOYSA-N 0.000 claims description 2
- KFDVPJUYSDEJTH-UHFFFAOYSA-N 4-ethenylpyridine Chemical compound C=CC1=CC=NC=C1 KFDVPJUYSDEJTH-UHFFFAOYSA-N 0.000 claims description 2
- 241000271566 Aves Species 0.000 claims description 2
- NOWKCMXCCJGMRR-UHFFFAOYSA-N Aziridine Chemical compound C1CN1 NOWKCMXCCJGMRR-UHFFFAOYSA-N 0.000 claims description 2
- 241000282465 Canis Species 0.000 claims description 2
- 239000004215 Carbon black (E152) Substances 0.000 claims description 2
- 241000283073 Equus caballus Species 0.000 claims description 2
- 241000282324 Felis Species 0.000 claims description 2
- GHAZCVNUKKZTLG-UHFFFAOYSA-N N-ethyl-succinimide Natural products CCN1C(=O)CCC1=O GHAZCVNUKKZTLG-UHFFFAOYSA-N 0.000 claims description 2
- HDFGOPSGAURCEO-UHFFFAOYSA-N N-ethylmaleimide Chemical compound CCN1C(=O)C=CC1=O HDFGOPSGAURCEO-UHFFFAOYSA-N 0.000 claims description 2
- 239000002168 alkylating agent Substances 0.000 claims description 2
- 229940100198 alkylating agent Drugs 0.000 claims description 2
- 229910052736 halogen Inorganic materials 0.000 claims description 2
- 229930195733 hydrocarbon Natural products 0.000 claims description 2
- 229910052740 iodine Inorganic materials 0.000 claims description 2
- JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 claims description 2
- QFRHEHPVTSCSIH-UHFFFAOYSA-N 2,2,2-trifluoro-n-(2-iodoethyl)acetamide Chemical compound FC(F)(F)C(=O)NCCI QFRHEHPVTSCSIH-UHFFFAOYSA-N 0.000 claims 1
- 229910052794 bromium Inorganic materials 0.000 claims 1
- 229910052801 chlorine Inorganic materials 0.000 claims 1
- 125000005843 halogen group Chemical group 0.000 claims 1
- LEBYISUPSSNHTJ-UHFFFAOYSA-N methoxy-methyl-oxo-sulfanylidene-$l^{6}-sulfane Chemical compound COS(C)(=O)=S LEBYISUPSSNHTJ-UHFFFAOYSA-N 0.000 claims 1
- 238000003860 storage Methods 0.000 abstract description 14
- 230000007774 longterm Effects 0.000 abstract description 9
- 238000004519 manufacturing process Methods 0.000 abstract description 8
- 238000002360 preparation method Methods 0.000 abstract description 2
- 239000003814 drug Substances 0.000 abstract 1
- 150000001413 amino acids Chemical group 0.000 description 27
- 235000001014 amino acid Nutrition 0.000 description 21
- 239000000243 solution Substances 0.000 description 14
- 108010006025 bovine growth hormone Proteins 0.000 description 11
- 108090000765 processed proteins & peptides Proteins 0.000 description 11
- 230000009467 reduction Effects 0.000 description 11
- 239000000872 buffer Substances 0.000 description 9
- 239000003795 chemical substances by application Substances 0.000 description 9
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 8
- 102000004196 processed proteins & peptides Human genes 0.000 description 8
- 238000004128 high performance liquid chromatography Methods 0.000 description 7
- 101000664737 Homo sapiens Somatotropin Proteins 0.000 description 6
- 241001465754 Metazoa Species 0.000 description 6
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 6
- 102000004142 Trypsin Human genes 0.000 description 6
- 108090000631 Trypsin Proteins 0.000 description 6
- 235000018417 cysteine Nutrition 0.000 description 6
- 239000012588 trypsin Substances 0.000 description 6
- 230000014759 maintenance of location Effects 0.000 description 5
- 239000000203 mixture Substances 0.000 description 5
- 108090000623 proteins and genes Proteins 0.000 description 5
- 235000019786 weight gain Nutrition 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 150000001945 cysteines Chemical class 0.000 description 4
- 238000001212 derivatisation Methods 0.000 description 4
- 230000007062 hydrolysis Effects 0.000 description 4
- 238000006460 hydrolysis reaction Methods 0.000 description 4
- 230000001817 pituitary effect Effects 0.000 description 4
- 229920001184 polypeptide Polymers 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 230000004584 weight gain Effects 0.000 description 4
- LEVWYRKDKASIDU-QWWZWVQMSA-N D-cystine Chemical compound OC(=O)[C@H](N)CSSC[C@@H](N)C(O)=O LEVWYRKDKASIDU-QWWZWVQMSA-N 0.000 description 3
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 3
- 241000700159 Rattus Species 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 229960003067 cystine Drugs 0.000 description 3
- 238000000502 dialysis Methods 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 3
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
- 241000251468 Actinopterygii Species 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 206010062767 Hypophysitis Diseases 0.000 description 2
- XYONNSVDNIRXKZ-UHFFFAOYSA-N S-methyl methanethiosulfonate Chemical compound CSS(C)(=O)=O XYONNSVDNIRXKZ-UHFFFAOYSA-N 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 230000027455 binding Effects 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 238000007623 carbamidomethylation reaction Methods 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- LEVWYRKDKASIDU-IMJSIDKUSA-N cystine group Chemical group C([C@@H](C(=O)O)N)SSC[C@@H](C(=O)O)N LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 2
- 239000003937 drug carrier Substances 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 230000000415 inactivating effect Effects 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 239000002953 phosphate buffered saline Substances 0.000 description 2
- 210000003635 pituitary gland Anatomy 0.000 description 2
- 238000000159 protein binding assay Methods 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000004007 reversed phase HPLC Methods 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 230000002194 synthesizing effect Effects 0.000 description 2
- JJVXHDTWVIPRBZ-VKHMYHEASA-N (2r)-2-[carboxy(methyl)amino]-3-sulfanylpropanoic acid Chemical compound OC(=O)N(C)[C@@H](CS)C(O)=O JJVXHDTWVIPRBZ-VKHMYHEASA-N 0.000 description 1
- DBIVLAVBOICUQX-UHFFFAOYSA-N 3-bromopropanamide Chemical compound NC(=O)CCBr DBIVLAVBOICUQX-UHFFFAOYSA-N 0.000 description 1
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 1
- NLHHRLWOUZZQLW-UHFFFAOYSA-N Acrylonitrile Chemical compound C=CC#N NLHHRLWOUZZQLW-UHFFFAOYSA-N 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 101000929799 Homo sapiens Acyl-CoA-binding protein Proteins 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- MQUQNUAYKLCRME-INIZCTEOSA-N N-tosyl-L-phenylalanyl chloromethyl ketone Chemical compound C1=CC(C)=CC=C1S(=O)(=O)N[C@H](C(=O)CCl)CC1=CC=CC=C1 MQUQNUAYKLCRME-INIZCTEOSA-N 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 241000656145 Thyrsites atun Species 0.000 description 1
- 108700001906 Tryptal Proteins 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000005054 agglomeration Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 229940124325 anabolic agent Drugs 0.000 description 1
- 239000003263 anabolic agent Substances 0.000 description 1
- 210000004198 anterior pituitary gland Anatomy 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 150000002009 diols Chemical class 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 230000004153 glucose metabolism Effects 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 150000002367 halogens Chemical group 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 239000011630 iodine Substances 0.000 description 1
- 229960004592 isopropanol Drugs 0.000 description 1
- 230000037356 lipid metabolism Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 229960001913 mecysteine Drugs 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 239000012299 nitrogen atmosphere Substances 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 238000012510 peptide mapping method Methods 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 108010057578 pregrowth hormone Proteins 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 230000009645 skeletal growth Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 210000005253 yeast cell Anatomy 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
- C07K14/575—Hormones
- C07K14/61—Growth hormone [GH], i.e. somatotropin
-
- 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)
- Endocrinology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Analytical Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Agricultural Chemicals And Associated Chemicals (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US07/242,542 US5079230A (en) | 1988-09-12 | 1988-09-12 | Stable bioactive somatotropins |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DD289544A5 true DD289544A5 (de) | 1991-05-02 |
Family
ID=22915193
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DD89332530A DD289544A5 (de) | 1988-09-12 | 1989-09-11 | Stabile bioaktive somatotropine |
Country Status (16)
| Country | Link |
|---|---|
| US (1) | US5079230A (ja) |
| EP (1) | EP0433395A1 (ja) |
| JP (1) | JPH04500519A (ja) |
| CN (1) | CN1037845C (ja) |
| AU (1) | AU4330889A (ja) |
| CA (1) | CA1339759C (ja) |
| DD (1) | DD289544A5 (ja) |
| ES (1) | ES2018397A6 (ja) |
| GR (1) | GR1002144B (ja) |
| HU (2) | HU206375B (ja) |
| NZ (1) | NZ230610A (ja) |
| PL (1) | PL162822B1 (ja) |
| RU (1) | RU2073686C1 (ja) |
| UA (1) | UA26853C2 (ja) |
| WO (1) | WO1990002758A1 (ja) |
| ZA (1) | ZA896914B (ja) |
Families Citing this family (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE68929273T2 (de) * | 1988-08-24 | 2001-07-05 | American Cyanamid Co., Wayne | Stabilisierung von Somatotropinen durch Modifikation von Cystein-Resten durch orts-spezifische Mutagenese oder chemische Derivatisierung |
| US5849694A (en) * | 1990-07-16 | 1998-12-15 | Synenki; Richard M. | Stable and bioactive modified porcine somatotropin and pharmaceutical compositions thereof |
| US5169834A (en) * | 1990-11-30 | 1992-12-08 | American Cyanamid Company | Compositions and method for reducing vial breakage during lyophilization |
| US5567620A (en) * | 1993-01-26 | 1996-10-22 | Eli Lilly And Company | Non-denaturing potency assay for somatotropin |
| ZA94169B (en) * | 1993-01-26 | 1994-09-07 | Lilly Co Eli | Non-denaturing potency assay for bovine somatotropin |
| DE4303744A1 (de) * | 1993-02-09 | 1994-08-11 | Univ Autonoma De Nuevo Leon Mo | Hundewachstumshormon |
| DK44593D0 (da) * | 1993-04-20 | 1993-04-20 | Novo Nordisk As | Fremgangsmaade til fremstilling af et polypeptid |
| ZA9711731B (en) * | 1996-12-31 | 1998-07-01 | Monsanto Co | Aqueous glycerol formulations of somatotropin |
| WO1998051296A1 (en) * | 1997-05-15 | 1998-11-19 | Schmidt Geoffrey J | Method of reducing immunological tolerance to malignancy |
| DK1775346T3 (da) * | 1997-06-25 | 2009-09-28 | Merck Serono Sa | Disulfid-tværbundne glycoproteinhormonanaloger, deres fremstilling og anvendelse |
| AU2001273388B2 (en) * | 2000-09-08 | 2005-01-13 | Gryphon Therapeutics, Inc. | "Pseudo"-native chemical ligation |
| US6811777B2 (en) * | 2002-04-13 | 2004-11-02 | Allan Mishra | Compositions and minimally invasive methods for treating incomplete connective tissue repair |
| DE60332358D1 (de) * | 2002-09-09 | 2010-06-10 | Hanall Pharmaceutical Co Ltd | Protease-resistente modifizierte interferon alpha polypeptide |
| US7998930B2 (en) | 2004-11-04 | 2011-08-16 | Hanall Biopharma Co., Ltd. | Modified growth hormones |
| WO2006121569A2 (en) | 2005-04-08 | 2006-11-16 | Neose Technologies, Inc. | Compositions and methods for the preparation of protease resistant human growth hormone glycosylation mutants |
| JP5875527B2 (ja) | 2010-01-22 | 2016-03-02 | ノヴォ・ノルディスク・ヘルス・ケア・アーゲー | ｉｎ−ｖｉｖｏにおける効力が延長された成長ホルモン |
| EP2446898A1 (en) | 2010-09-30 | 2012-05-02 | Laboratorios Del. Dr. Esteve, S.A. | Use of growth hormone to enhance the immune response in immunosuppressed patients |
| JP6464145B2 (ja) | 2013-04-05 | 2019-02-06 | ノヴォ・ノルディスク・ヘルス・ケア・アーゲー | 成長ホルモン化合物製剤 |
| CN108828237B (zh) * | 2018-08-24 | 2021-04-02 | 浙江理工大学 | 一种分析羊毛角蛋白中氨基酸键合折叠分布的方法 |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3853832A (en) * | 1971-04-27 | 1974-12-10 | Harmone Res Foundation | Synthetic human pituitary growth hormone and method of producing it |
| US4342832A (en) * | 1979-07-05 | 1982-08-03 | Genentech, Inc. | Method of constructing a replicable cloning vehicle having quasi-synthetic genes |
| JPS5630925A (en) * | 1979-08-21 | 1981-03-28 | Sumitomo Chem Co Ltd | Purification of human growth hormone |
| CA1224432A (en) * | 1982-08-17 | 1987-07-21 | Gary N. Buell | Dna sequences, recombinant dna molecules and processes for producing bovine growth hormone-like polypeptides in high yield |
| CA1341012C (en) * | 1982-09-27 | 2000-06-06 | Biogen, Inc. | Dna sequences, recombinant dna molecules and processes for producing swine growth hormone-like polypeptides |
| FI82266C (fi) * | 1982-10-19 | 1991-02-11 | Cetus Corp | Foerfarande foer framstaellning av il-2 -mutein. |
| US4620948A (en) * | 1982-12-22 | 1986-11-04 | Genentech, Inc. | Purification and activity assurance of precipitated heterologous proteins |
| WO1987000204A2 (en) * | 1985-06-26 | 1987-01-15 | The Upjohn Company | Purification of somatotropin from transformed microorganisms |
| US4766205A (en) * | 1985-11-13 | 1988-08-23 | Beatrice Companies, Inc. | Method for isolation of recombinant polypeptides in biologically active forms |
| US4816568A (en) * | 1986-05-16 | 1989-03-28 | International Minerals & Chemical Corp. | Stabilization of growth hormones |
| DE68929273T2 (de) * | 1988-08-24 | 2001-07-05 | American Cyanamid Co., Wayne | Stabilisierung von Somatotropinen durch Modifikation von Cystein-Resten durch orts-spezifische Mutagenese oder chemische Derivatisierung |
-
1988
- 1988-09-12 US US07/242,542 patent/US5079230A/en not_active Expired - Lifetime
-
1989
- 1989-08-09 CA CA000607863A patent/CA1339759C/en not_active Expired - Fee Related
- 1989-09-07 UA UA4895049A patent/UA26853C2/uk unknown
- 1989-09-07 JP JP1510357A patent/JPH04500519A/ja active Pending
- 1989-09-07 HU HU895729A patent/HU206375B/hu not_active IP Right Cessation
- 1989-09-07 EP EP89911168A patent/EP0433395A1/en not_active Withdrawn
- 1989-09-07 AU AU43308/89A patent/AU4330889A/en not_active Abandoned
- 1989-09-07 RU SU4895049/04A patent/RU2073686C1/ru not_active IP Right Cessation
- 1989-09-07 WO PCT/US1989/003871 patent/WO1990002758A1/en not_active Application Discontinuation
- 1989-09-08 GR GR890100562A patent/GR1002144B/el not_active IP Right Cessation
- 1989-09-11 CN CN89107230A patent/CN1037845C/zh not_active Expired - Fee Related
- 1989-09-11 NZ NZ230610A patent/NZ230610A/en unknown
- 1989-09-11 ZA ZA896914A patent/ZA896914B/xx unknown
- 1989-09-11 DD DD89332530A patent/DD289544A5/de unknown
- 1989-09-12 ES ES8903103A patent/ES2018397A6/es not_active Expired - Fee Related
- 1989-09-12 PL PL28138089A patent/PL162822B1/pl not_active IP Right Cessation
-
1991
- 1991-03-26 HU HU91787A patent/HU910787D0/hu unknown
Also Published As
| Publication number | Publication date |
|---|---|
| US5079230A (en) | 1992-01-07 |
| PL162822B1 (pl) | 1994-01-31 |
| CA1339759C (en) | 1998-03-17 |
| AU4330889A (en) | 1990-04-02 |
| ES2018397A6 (es) | 1991-04-01 |
| EP0433395A1 (en) | 1991-06-26 |
| JPH04500519A (ja) | 1992-01-30 |
| GR890100562A (el) | 1990-10-31 |
| HUT56856A (en) | 1991-10-28 |
| HU910787D0 (en) | 1991-09-30 |
| NZ230610A (en) | 1991-12-23 |
| GR1002144B (en) | 1996-02-16 |
| ZA896914B (en) | 1990-10-31 |
| WO1990002758A1 (en) | 1990-03-22 |
| RU2073686C1 (ru) | 1997-02-20 |
| CN1037845C (zh) | 1998-03-25 |
| HU206375B (en) | 1992-10-28 |
| UA26853C2 (uk) | 1999-12-29 |
| CN1041160A (zh) | 1990-04-11 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| IF04 | In force in the year 2004 |
Expiry date: 20090912 |