EP0433276A1 - Growth hormone related peptide - Google Patents

Growth hormone related peptide

Info

Publication number: EP0433276A1
Authority: EP; European Patent Office
Prior art keywords: growth hormone; molecule; activity; peptide; bgh
Prior art date: 1987-07-06
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 Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Withdrawn

Application number

EP19880905948

Other languages

German (de)

English (en)

French (fr)

Inventor

Roger Aston

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Teva Pharmaceuticals Australia Pty Ltd

Original Assignee

Peptide Technology Ltd

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.)

1987-07-06

Filing date

1988-07-06

Publication date

1991-06-26

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=27263482&utm_source=***_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=EP0433276(A1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1987-07-06 Priority claimed from GB878715866A external-priority patent/GB8715866D0/en

1987-07-06 Priority claimed from GB878715858A external-priority patent/GB8715858D0/en

1987-07-06 Priority claimed from GB878715859A external-priority patent/GB8715859D0/en

1988-07-06 Application filed by Peptide Technology Ltd filed Critical Peptide Technology Ltd

1991-06-26 Publication of EP0433276A1 publication Critical patent/EP0433276A1/en

Status Withdrawn legal-status Critical Current

Links

239000000122 growth hormone Substances 0.000 title claims abstract description 68
108010051696 Growth Hormone Proteins 0.000 title claims abstract description 56
102000018997 Growth Hormone Human genes 0.000 title claims abstract description 56
108090000765 processed proteins & peptides Proteins 0.000 title claims description 74
230000000694 effects Effects 0.000 claims abstract description 18
230000000890 antigenic effect Effects 0.000 claims abstract description 11
230000003054 hormonal effect Effects 0.000 claims description 21
239000000203 mixture Substances 0.000 claims description 17
238000000034 method Methods 0.000 claims description 13
239000012634 fragment Substances 0.000 claims description 10
239000000126 substance Substances 0.000 claims description 10
125000003275 alpha amino acid group Chemical group 0.000 claims description 9
238000002360 preparation method Methods 0.000 claims description 9
241000283690 Bos taurus Species 0.000 claims description 7
102000015636 Oligopeptides Human genes 0.000 claims description 7
108010038807 Oligopeptides Proteins 0.000 claims description 7
125000000539 amino acid group Chemical group 0.000 claims description 7
230000001737 promoting effect Effects 0.000 claims description 6
239000003795 chemical substances by application Substances 0.000 claims description 4
102000004169 proteins and genes Human genes 0.000 claims description 4
108090000623 proteins and genes Proteins 0.000 claims description 4
101000824878 Gallus gallus Somatotropin Proteins 0.000 claims description 3
241000251539 Vertebrata <Metazoa> Species 0.000 claims description 3
150000003839 salts Chemical class 0.000 claims description 3
230000015572 biosynthetic process Effects 0.000 abstract description 8
108010006025 bovine growth hormone Proteins 0.000 description 41
102000004196 processed proteins & peptides Human genes 0.000 description 34
241001494479 Pecora Species 0.000 description 32
241001465754 Metazoa Species 0.000 description 22
230000012010 growth Effects 0.000 description 20
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 20
238000011282 treatment Methods 0.000 description 16
108060003951 Immunoglobulin Proteins 0.000 description 15
102000018358 immunoglobulin Human genes 0.000 description 15
210000002966 serum Anatomy 0.000 description 13
108010058846 Ovalbumin Proteins 0.000 description 11
229940092253 ovalbumin Drugs 0.000 description 11
102000004877 Insulin Human genes 0.000 description 10
108090001061 Insulin Proteins 0.000 description 10
239000002671 adjuvant Substances 0.000 description 10
235000001014 amino acid Nutrition 0.000 description 10
230000002788 anti-peptide Effects 0.000 description 10
229940088597 hormone Drugs 0.000 description 10
239000005556 hormone Substances 0.000 description 10
229940125396 insulin Drugs 0.000 description 10
150000002632 lipids Chemical class 0.000 description 10
150000001413 amino acids Chemical class 0.000 description 8
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 8
239000002953 phosphate buffered saline Substances 0.000 description 8
229960005486 vaccine Drugs 0.000 description 8
241000699670 Mus sp. Species 0.000 description 7
210000004369 blood Anatomy 0.000 description 7
239000008280 blood Substances 0.000 description 7
238000003786 synthesis reaction Methods 0.000 description 7
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 6
DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 6
230000001904 diabetogenic effect Effects 0.000 description 6
238000010348 incorporation Methods 0.000 description 6
239000011347 resin Substances 0.000 description 6
229920005989 resin Polymers 0.000 description 6
241000894007 species Species 0.000 description 6
238000012360 testing method Methods 0.000 description 6
-1 9-fluorenyl- methoxycarbonyl (Fmoc) group Chemical group 0.000 description 5
HAYVTMHUNMMXCV-IMJSIDKUSA-N Cys-Ala Chemical group OC(=O)[C@H](C)NC(=O)[C@@H](N)CS HAYVTMHUNMMXCV-IMJSIDKUSA-N 0.000 description 5
SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 5
ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 5
210000000845 cartilage Anatomy 0.000 description 5
230000002708 enhancing effect Effects 0.000 description 5
238000002474 experimental method Methods 0.000 description 5
239000007924 injection Substances 0.000 description 5
238000002347 injection Methods 0.000 description 5
230000003647 oxidation Effects 0.000 description 5
238000007254 oxidation reaction Methods 0.000 description 5
238000003127 radioimmunoassay Methods 0.000 description 5
230000004044 response Effects 0.000 description 5
QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 4
241000283903 Ovis aries Species 0.000 description 4
102000007079 Peptide Fragments Human genes 0.000 description 4
108010033276 Peptide Fragments Proteins 0.000 description 4
239000002253 acid Substances 0.000 description 4
238000003556 assay Methods 0.000 description 4
210000004899 c-terminal region Anatomy 0.000 description 4
230000002163 immunogen Effects 0.000 description 4
238000004519 manufacturing process Methods 0.000 description 4
230000004060 metabolic process Effects 0.000 description 4
229940023041 peptide vaccine Drugs 0.000 description 4
239000007790 solid phase Substances 0.000 description 4
MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 3
YMWUJEATGCHHMB-UHFFFAOYSA-N Dichloromethane Chemical compound ClCCl YMWUJEATGCHHMB-UHFFFAOYSA-N 0.000 description 3
102000006395 Globulins Human genes 0.000 description 3
108010044091 Globulins Proteins 0.000 description 3
108010000521 Human Growth Hormone Proteins 0.000 description 3
102000002265 Human Growth Hormone Human genes 0.000 description 3
239000000854 Human Growth Hormone Substances 0.000 description 3
241000699666 Mus <mouse, genus> Species 0.000 description 3
101000836210 Mus musculus Somatotropin Proteins 0.000 description 3
101000868151 Rattus norvegicus Somatotropin Proteins 0.000 description 3
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
241000282887 Suidae Species 0.000 description 3
230000002942 anti-growth Effects 0.000 description 3
244000309466 calf Species 0.000 description 3
230000000875 corresponding effect Effects 0.000 description 3
230000008878 coupling Effects 0.000 description 3
238000010168 coupling process Methods 0.000 description 3
238000005859 coupling reaction Methods 0.000 description 3
238000009472 formulation Methods 0.000 description 3
238000002649 immunization Methods 0.000 description 3
239000007791 liquid phase Substances 0.000 description 3
210000004185 liver Anatomy 0.000 description 3
230000003389 potentiating effect Effects 0.000 description 3
235000018102 proteins Nutrition 0.000 description 3
229910052938 sodium sulfate Inorganic materials 0.000 description 3
235000011152 sodium sulphate Nutrition 0.000 description 3
230000009576 somatic growth Effects 0.000 description 3
229910021653 sulphate ion Inorganic materials 0.000 description 3
238000002255 vaccination Methods 0.000 description 3
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 2
108010088751 Albumins Proteins 0.000 description 2
102000009027 Albumins Human genes 0.000 description 2
241000972773 Aulopiformes Species 0.000 description 2
108091003079 Bovine Serum Albumin Proteins 0.000 description 2
CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
229920002307 Dextran Polymers 0.000 description 2
RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
238000002965 ELISA Methods 0.000 description 2
MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
241000283973 Oryctolagus cuniculus Species 0.000 description 2
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
NQRYJNQNLNOLGT-UHFFFAOYSA-N Piperidine Chemical compound C1CCNCC1 NQRYJNQNLNOLGT-UHFFFAOYSA-N 0.000 description 2
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
102100022831 Somatoliberin Human genes 0.000 description 2
101710142969 Somatoliberin Proteins 0.000 description 2
102000005157 Somatostatin Human genes 0.000 description 2
108010056088 Somatostatin Proteins 0.000 description 2
241000282898 Sus scrofa Species 0.000 description 2
AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
239000004473 Threonine Substances 0.000 description 2
238000004458 analytical method Methods 0.000 description 2
150000008064 anhydrides Chemical class 0.000 description 2
125000001797 benzyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])* 0.000 description 2
229940098773 bovine serum albumin Drugs 0.000 description 2
229910002092 carbon dioxide Inorganic materials 0.000 description 2
239000003054 catalyst Substances 0.000 description 2
239000001913 cellulose Substances 0.000 description 2
229920002678 cellulose Polymers 0.000 description 2
238000012412 chemical coupling Methods 0.000 description 2
230000021615 conjugation Effects 0.000 description 2
QTCANKDTWWSCMR-UHFFFAOYSA-N costic aldehyde Natural products C1CCC(=C)C2CC(C(=C)C=O)CCC21C QTCANKDTWWSCMR-UHFFFAOYSA-N 0.000 description 2
238000004132 cross linking Methods 0.000 description 2
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
238000010511 deprotection reaction Methods 0.000 description 2
238000000502 dialysis Methods 0.000 description 2
235000005911 diet Nutrition 0.000 description 2
230000037213 diet Effects 0.000 description 2
238000010790 dilution Methods 0.000 description 2
239000012895 dilution Substances 0.000 description 2
125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 2
238000004128 high performance liquid chromatography Methods 0.000 description 2
239000000413 hydrolysate Substances 0.000 description 2
230000005847 immunogenicity Effects 0.000 description 2
230000001976 improved effect Effects 0.000 description 2
238000001727 in vivo Methods 0.000 description 2
ISTFUJWTQAMRGA-UHFFFAOYSA-N iso-beta-costal Natural products C1C(C(=C)C=O)CCC2(C)CCCC(C)=C21 ISTFUJWTQAMRGA-UHFFFAOYSA-N 0.000 description 2
230000006651 lactation Effects 0.000 description 2
230000004132 lipogenesis Effects 0.000 description 2
230000003520 lipogenic effect Effects 0.000 description 2
239000000463 material Substances 0.000 description 2
230000002503 metabolic effect Effects 0.000 description 2
WXEHBUMAEPOYKP-UHFFFAOYSA-N methylsulfanylethane Chemical compound CCSC WXEHBUMAEPOYKP-UHFFFAOYSA-N 0.000 description 2
102000013415 peroxidase activity proteins Human genes 0.000 description 2
108040007629 peroxidase activity proteins Proteins 0.000 description 2
229920000642 polymer Polymers 0.000 description 2
238000001556 precipitation Methods 0.000 description 2
238000002203 pretreatment Methods 0.000 description 2
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
125000006239 protecting group Chemical group 0.000 description 2
235000019515 salmon Nutrition 0.000 description 2
238000003307 slaughter Methods 0.000 description 2
239000011780 sodium chloride Substances 0.000 description 2
239000000243 solution Substances 0.000 description 2
NHXLMOGPVYXJNR-ATOGVRKGSA-N somatostatin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C3=CC=CC=C3NC=2)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N1)[C@@H](C)O)NC(=O)CNC(=O)[C@H](C)N)C(O)=O)=O)[C@H](O)C)C1=CC=CC=C1 NHXLMOGPVYXJNR-ATOGVRKGSA-N 0.000 description 2
229960000553 somatostatin Drugs 0.000 description 2
210000004003 subcutaneous fat Anatomy 0.000 description 2
239000007929 subcutaneous injection Substances 0.000 description 2
238000010254 subcutaneous injection Methods 0.000 description 2
125000005931 tert-butyloxycarbonyl group Chemical group [H]C([H])([H])C(OC(*)=O)(C([H])([H])[H])C([H])([H])[H] 0.000 description 2
238000004809 thin layer chromatography Methods 0.000 description 2
210000001519 tissue Anatomy 0.000 description 2
210000002268 wool Anatomy 0.000 description 2
ASOKPJOREAFHNY-UHFFFAOYSA-N 1-Hydroxybenzotriazole Chemical compound C1=CC=C2N(O)N=NC2=C1 ASOKPJOREAFHNY-UHFFFAOYSA-N 0.000 description 1
LIEVTTYXDCZXRG-UHFFFAOYSA-N 2,3,4-trinitrobenzenesulfonic acid Chemical compound OS(=O)(=O)C1=CC=C([N+]([O-])=O)C([N+]([O-])=O)=C1[N+]([O-])=O LIEVTTYXDCZXRG-UHFFFAOYSA-N 0.000 description 1
HJBLUNHMOKFZQX-UHFFFAOYSA-N 3-hydroxy-1,2,3-benzotriazin-4-one Chemical compound C1=CC=C2C(=O)N(O)N=NC2=C1 HJBLUNHMOKFZQX-UHFFFAOYSA-N 0.000 description 1
CLCPDSJUXHDRGX-UHFFFAOYSA-N 6-(1,3-dihydroxyisobutyl)thymine Chemical class CC1=C(CC(CO)CO)NC(=O)NC1=O CLCPDSJUXHDRGX-UHFFFAOYSA-N 0.000 description 1
239000004475 Arginine Substances 0.000 description 1
101001075376 Bos taurus Gamma-glutamyl hydrolase Proteins 0.000 description 1
NLZUEZXRPGMBCV-UHFFFAOYSA-N Butylhydroxytoluene Chemical compound CC1=CC(C(C)(C)C)=C(O)C(C(C)(C)C)=C1 NLZUEZXRPGMBCV-UHFFFAOYSA-N 0.000 description 1
206010053567 Coagulopathies Diseases 0.000 description 1
208000034656 Contusions Diseases 0.000 description 1
235000019750 Crude protein Nutrition 0.000 description 1
241000283073 Equus caballus Species 0.000 description 1
101000664736 Equus caballus Somatotropin Proteins 0.000 description 1
KRHYYFGTRYWZRS-UHFFFAOYSA-N Fluorane Chemical compound F KRHYYFGTRYWZRS-UHFFFAOYSA-N 0.000 description 1
241000287828 Gallus gallus Species 0.000 description 1
101000993347 Gallus gallus Ciliary neurotrophic factor Proteins 0.000 description 1
101100366203 Gallus gallus GH gene Proteins 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
239000000095 Growth Hormone-Releasing Hormone Substances 0.000 description 1
229940122853 Growth hormone antagonist Drugs 0.000 description 1
108091006905 Human Serum Albumin Proteins 0.000 description 1
102000008100 Human Serum Albumin Human genes 0.000 description 1
208000013016 Hypoglycemia Diseases 0.000 description 1
OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
239000004472 Lysine Substances 0.000 description 1
101001075372 Mus musculus Gamma-glutamyl hydrolase Proteins 0.000 description 1
102000015731 Peptide Hormones Human genes 0.000 description 1
108010038988 Peptide Hormones Proteins 0.000 description 1
101001075370 Rattus norvegicus Gamma-glutamyl hydrolase Proteins 0.000 description 1
108020004511 Recombinant DNA Proteins 0.000 description 1
241000277331 Salmonidae Species 0.000 description 1
238000000692 Student's t-test Methods 0.000 description 1
QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
230000010933 acylation Effects 0.000 description 1
238000005917 acylation reaction Methods 0.000 description 1
XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 1
229910052782 aluminium Inorganic materials 0.000 description 1
239000004411 aluminium Substances 0.000 description 1
150000003862 amino acid derivatives Chemical class 0.000 description 1
RDOXTESZEPMUJZ-UHFFFAOYSA-N anisole Chemical compound COC1=CC=CC=C1 RDOXTESZEPMUJZ-UHFFFAOYSA-N 0.000 description 1
230000003388 anti-hormonal effect Effects 0.000 description 1
230000003302 anti-idiotype Effects 0.000 description 1
230000005875 antibody response Effects 0.000 description 1
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
235000003704 aspartic acid Nutrition 0.000 description 1
150000001510 aspartic acids Chemical class 0.000 description 1
230000001580 bacterial effect Effects 0.000 description 1
102000005936 beta-Galactosidase Human genes 0.000 description 1
108010005774 beta-Galactosidase Proteins 0.000 description 1
230000004071 biological effect Effects 0.000 description 1
239000000872 buffer Substances 0.000 description 1
238000004364 calculation method Methods 0.000 description 1
150000001718 carbodiimides Chemical class 0.000 description 1
239000001569 carbon dioxide Substances 0.000 description 1
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
150000001735 carboxylic acids Chemical class 0.000 description 1
239000000969 carrier Substances 0.000 description 1
238000005119 centrifugation Methods 0.000 description 1
238000004587 chromatography analysis Methods 0.000 description 1
239000007979 citrate buffer Substances 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
230000035602 clotting Effects 0.000 description 1
230000000536 complexating effect Effects 0.000 description 1
230000002596 correlated effect Effects 0.000 description 1
239000007822 coupling agent Substances 0.000 description 1
239000003431 cross linking reagent Substances 0.000 description 1
235000018417 cysteine Nutrition 0.000 description 1
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
230000003247 decreasing effect Effects 0.000 description 1
AQEFLFZSWDEAIP-UHFFFAOYSA-N di-tert-butyl ether Chemical class CC(C)(C)OC(C)(C)C AQEFLFZSWDEAIP-UHFFFAOYSA-N 0.000 description 1
BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
229910000397 disodium phosphate Inorganic materials 0.000 description 1
235000019800 disodium phosphate Nutrition 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
238000004945 emulsification Methods 0.000 description 1
239000012467 final product Substances 0.000 description 1
235000013305 food Nutrition 0.000 description 1
238000004108 freeze drying Methods 0.000 description 1
238000002523 gelfiltration Methods 0.000 description 1
239000008103 glucose Substances 0.000 description 1
235000013922 glutamic acid Nutrition 0.000 description 1
239000004220 glutamic acid Substances 0.000 description 1
244000144993 groups of animals Species 0.000 description 1
125000002795 guanidino group Chemical group C(N)(=N)N* 0.000 description 1
HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
125000004356 hydroxy functional group Chemical group O* 0.000 description 1
230000002218 hypoglycaemic effect Effects 0.000 description 1
230000016784 immunoglobulin production Effects 0.000 description 1
229940072221 immunoglobulins Drugs 0.000 description 1
238000002513 implantation Methods 0.000 description 1
230000001939 inductive effect Effects 0.000 description 1
239000003112 inhibitor Substances 0.000 description 1
238000007918 intramuscular administration Methods 0.000 description 1
239000007927 intramuscular injection Substances 0.000 description 1
239000007928 intraperitoneal injection Substances 0.000 description 1
238000010253 intravenous injection Methods 0.000 description 1
238000004255 ion exchange chromatography Methods 0.000 description 1
150000002500 ions Chemical class 0.000 description 1
108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
230000004130 lipolysis Effects 0.000 description 1
230000002366 lipolytic effect Effects 0.000 description 1
125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
238000013507 mapping Methods 0.000 description 1
235000013372 meat Nutrition 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
210000003205 muscle Anatomy 0.000 description 1
PSHKMPUSSFXUIA-UHFFFAOYSA-N n,n-dimethylpyridin-2-amine Chemical compound CN(C)C1=CC=CC=N1 PSHKMPUSSFXUIA-UHFFFAOYSA-N 0.000 description 1
238000006386 neutralization reaction Methods 0.000 description 1
125000000538 pentafluorophenyl group Chemical group FC1=C(F)C(F)=C(*)C(F)=C1F 0.000 description 1
239000000813 peptide hormone Substances 0.000 description 1
238000010647 peptide synthesis reaction Methods 0.000 description 1
239000002504 physiological saline solution Substances 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
239000013641 positive control Substances 0.000 description 1
238000000746 purification Methods 0.000 description 1
239000001397 quillaja saponaria molina bark Substances 0.000 description 1
239000002516 radical scavenger Substances 0.000 description 1
239000000700 radioactive tracer Substances 0.000 description 1
239000003488 releasing hormone Substances 0.000 description 1
230000003252 repetitive effect Effects 0.000 description 1
230000004043 responsiveness Effects 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
229930182490 saponin Natural products 0.000 description 1
150000007949 saponins Chemical class 0.000 description 1
230000007017 scission Effects 0.000 description 1
AJPJDKMHJJGVTQ-UHFFFAOYSA-M sodium dihydrogen phosphate Chemical compound [Na+].OP(O)([O-])=O AJPJDKMHJJGVTQ-UHFFFAOYSA-M 0.000 description 1
210000004872 soft tissue Anatomy 0.000 description 1
238000002764 solid phase assay Methods 0.000 description 1
239000002904 solvent Substances 0.000 description 1
210000001562 sternum Anatomy 0.000 description 1
230000004936 stimulating effect Effects 0.000 description 1
238000006467 substitution reaction Methods 0.000 description 1
239000000758 substrate Substances 0.000 description 1
230000001629 suppression Effects 0.000 description 1
238000010998 test 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
HNKJADCVZUBCPG-UHFFFAOYSA-N thioanisole Chemical compound CSC1=CC=CC=C1 HNKJADCVZUBCPG-UHFFFAOYSA-N 0.000 description 1
230000034005 thiol-disulfide exchange Effects 0.000 description 1
UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 1
125000002221 trityl group Chemical group [H]C1=C([H])C([H])=C([H])C([H])=C1C([*])(C1=C(C(=C(C(=C1[H])[H])[H])[H])[H])C1=C([H])C([H])=C([H])C([H])=C1[H] 0.000 description 1
OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
238000012762 unpaired Student’s t-test Methods 0.000 description 1
230000003442 weekly effect Effects 0.000 description 1
238000005303 weighing Methods 0.000 description 1
230000004584 weight gain Effects 0.000 description 1
235000019786 weight gain Nutrition 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/26—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against hormones ; against hormone releasing or inhibiting factors
- 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

Definitions

the peptide will generally be antigenic and capable of stimulating the production of antibodies which, when in an appropriate formulation, potentiate the effect of growth hormone.
Figure 2 clearly shows enhancement of dwarf mouse growth rate by anti GH antisera, as determined by 35 S 24
Sheep Pure Poll Dorset
the four groups were subjected to a pre-treatment period of 3 weeks and weighed twice per week.
blood was also taken at the times of weighing.
blood samples were taken hourly for 18 hours from a catheter.
an insulin tolerance test was performed on the animals. All animals were maintained on an ad lib diet of 16% crude protein farm mix (daily refusals were recorded) .

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Endocrinology (AREA)
Life Sciences & Earth Sciences (AREA)
Molecular Biology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Genetics & Genomics (AREA)
Medicinal Chemistry (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Gastroenterology & Hepatology (AREA)
Zoology (AREA)
Toxicology (AREA)
Immunology (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)

EP19880905948 1987-07-06 1988-07-06 Growth hormone related peptide Withdrawn EP0433276A1 (en)

Applications Claiming Priority (6)

Application Number	Priority Date	Filing Date	Title
GB8715866		1987-07-06
GB878715866A GB8715866D0 (en)	1987-07-06	1987-07-06	Peptides
GB878715858A GB8715858D0 (en)	1987-07-06	1987-07-06	Peptides
GB8715859		1987-07-06
GB8715858		1987-07-06
GB878715859A GB8715859D0 (en)	1987-07-06	1987-07-06	Peptides

Publications (1)

Publication Number	Publication Date
EP0433276A1 true EP0433276A1 (en)	1991-06-26

Family

ID=27263482

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
EP19880905948 Withdrawn EP0433276A1 (en)	1987-07-06	1988-07-06	Growth hormone related peptide

Country Status (6)

Country	Link
EP (1)	EP0433276A1 (da)
JP (1)	JPH03503403A (da)
AU (1)	AU630591B2 (da)
DK (1)	DK4390A (da)
FI (1)	FI900075A (da)
WO (1)	WO1989000166A2 (da)

Families Citing this family (8)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5210180A (en) *	1989-10-27	1993-05-11	American Cyanamid Company	Enhancement of porcine somatotropin activity
US6165465A (en) *	1990-05-15	2000-12-26	American Cyanamid Company	Immunologic enhancement of the somatogenic effect of somatotropin with an antibody
US5543390A (en)	1990-11-01	1996-08-06	State Of Oregon, Acting By And Through The Oregon State Board Of Higher Education, Acting For And On Behalf Of The Oregon Health Sciences University	Covalent microparticle-drug conjugates for biological targeting
US5827819A (en)	1990-11-01	1998-10-27	Oregon Health Sciences University	Covalent polar lipid conjugates with neurologically active compounds for targeting
US5426096A (en) *	1992-03-18	1995-06-20	Soenksen; Peter	Use of human growth hormone
US5338836A (en) *	1992-07-29	1994-08-16	American Cyanamid Company	Biologically active porcine somatotropin polypeptides and methods of using the same
AU4986393A (en) *	1992-08-19	1994-03-15	Massey University	Methods for effecting a prolonged reduction in measurable fat content and medicaments for use therein
AU2003297953B2 (en) *	2002-09-05	2009-02-26	Resistentia Pharmaceuticals Ab	Allergy vaccines

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
FI83662C (fi) *	1980-07-17	1991-08-12	Scripps Clinic Res	Diagnostik antikropp och foerfarande foer dess framstaellning.

1988
- 1988-07-06 AU AU19672/88A patent/AU630591B2/en not_active Withdrawn - After Issue
- 1988-07-06 JP JP50554188A patent/JPH03503403A/ja active Pending
- 1988-07-06 WO PCT/GB1988/000528 patent/WO1989000166A2/en not_active Application Discontinuation
- 1988-07-06 EP EP19880905948 patent/EP0433276A1/en not_active Withdrawn
1990
- 1990-01-05 FI FI900075A patent/FI900075A/fi not_active IP Right Cessation
- 1990-01-08 DK DK004390A patent/DK4390A/da not_active Application Discontinuation

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO8900166A2 *

Also Published As

Publication number	Publication date
WO1989000166A3 (en)	1989-01-26
WO1989000166A2 (en)	1989-01-12
FI900075A0 (fi)	1990-01-05
AU1967288A (en)	1989-01-30
FI900075A (fi)	1990-01-05
DK4390A (da)	1990-03-05
DK4390D0 (da)	1990-01-08
AU630591B2 (en)	1992-11-05
JPH03503403A (ja)	1991-08-01

Legal Events

Date	Code	Title	Description
1991-05-09	PUAI	Public reference made under article 153(3) epc to a published international application that has entered the european phase	Free format text: ORIGINAL CODE: 0009012
1991-06-26	17P	Request for examination filed	Effective date: 19891227
1991-06-26	AK	Designated contracting states	Kind code of ref document: A1 Designated state(s): AT BE CH DE FR GB IT LI LU NL SE
1992-10-07	17Q	First examination report despatched	Effective date: 19920820
1994-04-27	STAA	Information on the status of an ep patent application or granted ep patent	Free format text: STATUS: THE APPLICATION IS DEEMED TO BE WITHDRAWN
1994-06-15	18D	Application deemed to be withdrawn	Effective date: 19931214

Publication	Publication Date	Title
JPH10512881A (ja)	1998-12-08	成長ホルモン放出ホルモンの新規な非常に効力のあるアゴニスト
JP6375089B2 (ja)	2018-08-15	強力なアゴニスト作用を有する新規なｇｈ−ｒｈ類似体
AU622858B2 (en)	1992-04-30	Biologically active molecules
AU630591B2 (en)	1992-11-05	Growth hormone related peptide
AP71A (en)	1990-02-24	Peptide structures, immunogens containing them and their uses in the control of fertility.
AU674881B2 (en)	1997-01-16	Growth hormone potentiating molecules
EP0303488B1 (en)	1994-12-28	Biologically active molecules
JPH06504537A (ja)	1994-05-26	魚のｌｈｒｈ類似体
JP2000509964A (ja)	2000-08-08	成長ホルモン生物活性に対して増強作用を有する生物活性分子、特にペプチド
AU649399B2 (en)	1994-05-26	GRF peptides
DK173981B1 (da)	2002-03-25	Farmaceutisk antigenetisk formulering