DD289544A5 - Stabile bioaktive somatotropine - Google Patents

Stabile bioaktive somatotropine Download PDF

Info

Publication number: DD289544A5
Authority: DD; German Democratic Republic
Prior art keywords: somatotropin; small loop; derivatized; sulfhydryl groups; loop
Prior art date: 1988-09-12

Application number

DD89332530A

Other languages

German (de)

English (en)

Inventor

Zafar I Randawa

James E Seely

Original Assignee

Pitman-Moore,Inc.,Us

Priority date (The priority date 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 date listed.)

1988-09-12

Filing date

1989-09-11

Publication date

1991-05-02

1989-09-11 Application filed by Pitman-Moore,Inc.,Us filed Critical Pitman-Moore,Inc.,Us

1991-05-02 Publication of DD289544A5 publication Critical patent/DD289544A5/de

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)
Chemical Kinetics & Catalysis (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Endocrinology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Genetics & Genomics (AREA)
Medicinal Chemistry (AREA)
Molecular Biology (AREA)
Gastroenterology & Hepatology (AREA)
Toxicology (AREA)
Zoology (AREA)
General Chemical & Material Sciences (AREA)
Analytical Chemistry (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Agricultural Chemicals And Associated Chemicals (AREA)

DD89332530A 1988-09-12 1989-09-11 Stabile bioaktive somatotropine DD289544A5 (de)

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)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
ATE198353T1 (de) *	1988-08-24	2001-01-15	American Cyanamid Co	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
AU7493198A (en) *	1997-05-15	1998-12-08	Geoffrey J Schmidt	Method of reducing immunological tolerance to malignancy
SI0996629T1 (sl) *	1997-06-25	2006-12-31	Applied Research Systems	Analogi glikoproteinskega hormona povezanega z disulfidi, priprava in uporaba
EE200300089A (et) *	2000-09-08	2005-02-15	Gryphon Therapeutics, Inc.	Sünteetilised erütropoeesi stimuleerivad valgud, nende valmistamismeetodid ning kasutamine
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
US20070154992A1 (en)	2005-04-08	2007-07-05	Neose Technologies, Inc.	Compositions and methods for the preparation of protease resistant human growth hormone glycosylation mutants
CN118767117A (zh)	2010-01-22	2024-10-15	诺沃—诺迪斯克保健股份有限公司	体内功效延长的生长激素
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
US11045523B2 (en)	2013-04-05	2021-06-29	Novo Nordisk Healthcare Ag	Formulation of growth hormone albumin-binder conjugate
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)

* Cited by examiner, † Cited by third party
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
DE3685424D1 (de) *	1985-06-26	1992-06-25	Upjohn Co	Solubilisation und oxidation von somatotropin aus transformierten mikroorganismen.
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
ATE198353T1 (de) *	1988-08-24	2001-01-15	American Cyanamid Co	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 HU HU895729A patent/HU206375B/hu not_active IP Right Cessation
- 1989-09-07 AU AU43308/89A patent/AU4330889A/en not_active Abandoned
- 1989-09-07 WO PCT/US1989/003871 patent/WO1990002758A1/en not_active Ceased
- 1989-09-07 RU SU4895049/04A patent/RU2073686C1/ru not_active IP Right Cessation
- 1989-09-07 JP JP1510357A patent/JPH04500519A/ja active Pending
- 1989-09-07 EP EP89911168A patent/EP0433395A1/en not_active Withdrawn
- 1989-09-07 UA UA4895049A patent/UA26853C2/uk unknown
- 1989-09-08 GR GR890100562A patent/GR1002144B/el not_active IP Right Cessation
- 1989-09-11 NZ NZ230610A patent/NZ230610A/en unknown
- 1989-09-11 CN CN89107230A patent/CN1037845C/zh not_active Expired - Fee Related
- 1989-09-11 DD DD89332530A patent/DD289544A5/de unknown
- 1989-09-11 ZA ZA896914A patent/ZA896914B/xx unknown
- 1989-09-12 PL PL28138089A patent/PL162822B1/pl not_active IP Right Cessation
- 1989-09-12 ES ES8903103A patent/ES2018397A6/es not_active Expired - Lifetime
1991
- 1991-03-26 HU HU91787A patent/HU910787D0/hu unknown

Also Published As

Publication number	Publication date
PL162822B1 (pl)	1994-01-31
EP0433395A1 (en)	1991-06-26
GR1002144B (en)	1996-02-16
CA1339759C (en)	1998-03-17
RU2073686C1 (ru)	1997-02-20
ZA896914B (en)	1990-10-31
HU910787D0 (en)	1991-09-30
CN1037845C (zh)	1998-03-25
GR890100562A (el)	1990-10-31
NZ230610A (en)	1991-12-23
HUT56856A (en)	1991-10-28
ES2018397A6 (es)	1991-04-01
US5079230A (en)	1992-01-07
CN1041160A (zh)	1990-04-11
WO1990002758A1 (en)	1990-03-22
JPH04500519A (ja)	1992-01-30
AU4330889A (en)	1990-04-02
UA26853C2 (uk)	1999-12-29
HU206375B (en)	1992-10-28

Legal Events

Date	Code	Title	Description
2004-04-28	IF04	In force in the year 2004	Expiry date: 20090912

Publication	Publication Date	Title
DD289544A5 (de)	1991-05-02	Stabile bioaktive somatotropine
DE3852383T2 (de)	1995-04-20	Gereinigtes follikel-stimulierendes hormon.
DE3650055T2 (de)	1994-12-15	Fibroblast-wachstumsfaktor.
EP1161452B1 (de)	2009-04-15	Kovalent verbrückte insulindimere
DE3852033T2 (de)	1995-04-27	Follistatin und verfahren zur reinigung desselben.
DE69534852T2 (de)	2006-09-21	Verbesserte zyclische crf agonisten
DE3855536T2 (de)	1997-02-27	Rezeptoren für wachstumshormone
DE19735711C2 (de)	2001-04-26	Verfahren zur Herstellung eines Vorläufers von Insulin oder Insulinderivaten mit korrekt verbundenen Cystinbrücken
DE69108830T2 (de)	1995-09-14	Neue im schwein vorkommende physiologisch aktive peptide.
DE60102899T2 (de)	2005-03-31	Verfahren zur lösung von glucagon-ähnlichen peptid-1 (glp-1) verbindungen
DE69018461T2 (de)	1995-08-03	Hepatospezifische insulin-analoga.
DE3485945T2 (de)	1993-06-17	Gereinigter transformierender wachstum-beta-faktor aus humanen plaketten und plazenten stammend.
DE3650088T2 (de)	1995-01-26	Inhibin und dessen reinigung.
DE3587164T2 (de)	1993-07-15	Antidiabetikaverbindungen.
EP0056951B1 (de)	1985-06-19	Verfahren zur Herstellung von Humaninsulin oder dessen Derivaten aus Schweineinsulin oder dessen Derivaten
EP0376156A2 (de)	1990-07-04	Neue Insulinderivate, Verfahren zu deren Herstellung, ihre Verwendung und eine sie enthaltende pharmazeutische Zubereitung
WO1986003493A1 (fr)	1986-06-19	Hirudine-pa et ses derives, leur procede de production et leur utilisation
DE3878231T2 (de)	1993-05-27	Neues cadiodilatin-fragment, prozess zu dessen herstellung und dessen anwendung.
DE3887338T2 (de)	1994-05-05	Superaktive menschliche insulin-analoge.
DE3587227T2 (de)	1993-08-12	Antidiabetikaverbindungen.
EP1084248B1 (de)	2006-07-26	Neue insulinanaloga mit erhöhter zinkbindung
DE69637464T2 (de)	2008-11-06	Therapeutische fragmente des "von willebrand" faktors
DE3587226T2 (de)	1993-08-05	Antidiabetikaverbindungen.
EP0089007B1 (de)	1986-07-30	Verfahren zur Umwandlung von Präproinsulinanaloga zu Insulinen
DE3788170T2 (de)	1994-04-07	Methode zur Reinigung und Isolierung von zwei ionischen Formen von Somatomedin.