AU620673B2 - Somatotropin analogs - Google Patents

Somatotropin analogs

Info

Publication number: AU620673B2
Authority: AU; Australia
Prior art keywords: bst; somatotropin; serine; mammalian; vector
Prior art date: 1989-01-31
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.): Ceased

Application number

AU46631/89A

Other languages

English (en)

Other versions

AU4663189A (en

Inventor

John E. Mott

Alan J. Parcells

Che-Shen C. Tomich

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.)

Pharmacia and Upjohn Co

Original Assignee

Upjohn Co

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.)

1989-01-31

Filing date

1989-12-11

Publication date

1992-02-20

1989-12-11 Application filed by Upjohn Co filed Critical Upjohn Co

1990-08-24 Publication of AU4663189A publication Critical patent/AU4663189A/en

1992-02-20 Application granted granted Critical

1992-02-20 Publication of AU620673B2 publication Critical patent/AU620673B2/en

1997-04-24 Assigned to PHARMACIA & UPJOHN COMPANY reassignment PHARMACIA & UPJOHN COMPANY Request to Amend Deed and Register Assignors: UPJOHN COMPANY, THE

2009-12-11 Anticipated expiration legal-status Critical

Status Ceased legal-status Critical Current

Links

108010051696 Growth Hormone Proteins 0.000 title claims description 38
102000018997 Growth Hormone Human genes 0.000 title claims description 38
239000013598 vector Substances 0.000 claims description 82
108090000623 proteins and genes Proteins 0.000 claims description 70
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 57
241001465754 Metazoa Species 0.000 claims description 34
125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 claims description 34
241000283690 Bos taurus Species 0.000 claims description 28
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 28
238000000034 method Methods 0.000 claims description 21
235000018102 proteins Nutrition 0.000 claims description 21
102000004169 proteins and genes Human genes 0.000 claims description 21
108010006025 bovine growth hormone Proteins 0.000 claims description 17
235000013336 milk Nutrition 0.000 claims description 12
239000008267 milk Substances 0.000 claims description 12
210000004080 milk Anatomy 0.000 claims description 12
244000005700 microbiome Species 0.000 claims description 8
239000000203 mixture Substances 0.000 claims description 8
241000894007 species Species 0.000 claims description 8
235000013365 dairy product Nutrition 0.000 claims description 7
238000004519 manufacturing process Methods 0.000 claims description 6
230000001965 increasing effect Effects 0.000 claims description 5
241000282849 Ruminantia Species 0.000 claims description 4
241000588722 Escherichia Species 0.000 claims description 2
230000001580 bacterial effect Effects 0.000 claims description 2
230000002708 enhancing effect Effects 0.000 claims description 2
239000012634 fragment Substances 0.000 description 68
108020004414 DNA Proteins 0.000 description 30
108020004705 Codon Proteins 0.000 description 25
210000004027 cell Anatomy 0.000 description 23
239000013612 plasmid Substances 0.000 description 22
235000018417 cysteine Nutrition 0.000 description 20
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 18
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 15
238000010276 construction Methods 0.000 description 14
241000700159 Rattus Species 0.000 description 13
235000001014 amino acid Nutrition 0.000 description 13
108091034117 Oligonucleotide Proteins 0.000 description 12
230000000875 corresponding effect Effects 0.000 description 12
125000003275 alpha amino acid group Chemical group 0.000 description 10
238000010367 cloning Methods 0.000 description 10
239000002299 complementary DNA Substances 0.000 description 10
238000002360 preparation method Methods 0.000 description 10
150000001413 amino acids Chemical class 0.000 description 9
238000006243 chemical reaction Methods 0.000 description 8
101150066555 lacZ gene Proteins 0.000 description 8
239000000872 buffer Substances 0.000 description 7
238000012163 sequencing technique Methods 0.000 description 7
101150108727 trpl gene Proteins 0.000 description 7
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
241000588724 Escherichia coli Species 0.000 description 6
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 6
108091028043 Nucleic acid sequence Proteins 0.000 description 6
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 6
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
125000000539 amino acid group Chemical group 0.000 description 6
238000002347 injection Methods 0.000 description 6
239000007924 injection Substances 0.000 description 6
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 5
206010062767 Hypophysitis Diseases 0.000 description 5
235000015278 beef Nutrition 0.000 description 5
230000008859 change Effects 0.000 description 5
150000001945 cysteines Chemical class 0.000 description 5
210000003635 pituitary gland Anatomy 0.000 description 5
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
239000000243 solution Substances 0.000 description 5
238000012360 testing method Methods 0.000 description 5
RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 4
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 4
102000004190 Enzymes Human genes 0.000 description 4
108090000790 Enzymes Proteins 0.000 description 4
241000124008 Mammalia Species 0.000 description 4
UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 4
108010005774 beta-Galactosidase Proteins 0.000 description 4
238000004166 bioassay Methods 0.000 description 4
230000004071 biological effect Effects 0.000 description 4
230000037396 body weight Effects 0.000 description 4
150000001875 compounds Chemical class 0.000 description 4
230000000694 effects Effects 0.000 description 4
229940088598 enzyme Drugs 0.000 description 4
239000000499 gel Substances 0.000 description 4
230000006651 lactation Effects 0.000 description 4
230000001817 pituitary effect Effects 0.000 description 4
108090000765 processed proteins & peptides Proteins 0.000 description 4
239000000523 sample Substances 0.000 description 4
238000006467 substitution reaction Methods 0.000 description 4
230000009466 transformation Effects 0.000 description 4
CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 3
108091026890 Coding region Proteins 0.000 description 3
102000053602 DNA Human genes 0.000 description 3
108020005187 Oligonucleotide Probes Proteins 0.000 description 3
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 3
229960000723 ampicillin Drugs 0.000 description 3
235000011089 carbon dioxide Nutrition 0.000 description 3
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
238000005119 centrifugation Methods 0.000 description 3
230000029087 digestion Effects 0.000 description 3
238000009396 hybridization Methods 0.000 description 3
239000007943 implant Substances 0.000 description 3
230000006698 induction Effects 0.000 description 3
238000003780 insertion Methods 0.000 description 3
230000037431 insertion Effects 0.000 description 3
238000002955 isolation Methods 0.000 description 3
229910001629 magnesium chloride Inorganic materials 0.000 description 3
230000004048 modification Effects 0.000 description 3
238000012986 modification Methods 0.000 description 3
239000000178 monomer Substances 0.000 description 3
230000035772 mutation Effects 0.000 description 3
239000002751 oligonucleotide probe Substances 0.000 description 3
239000000047 product Substances 0.000 description 3
238000011160 research Methods 0.000 description 3
238000003307 slaughter Methods 0.000 description 3
239000011780 sodium chloride Substances 0.000 description 3
KSAVQLQVUXSOCR-UHFFFAOYSA-M sodium lauroyl sarcosinate Chemical compound [Na+].CCCCCCCCCCCC(=O)N(C)CC([O-])=O KSAVQLQVUXSOCR-UHFFFAOYSA-M 0.000 description 3
210000001519 tissue Anatomy 0.000 description 3
238000005406 washing Methods 0.000 description 3
OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 2
229920002271 DEAE-Sepharose Polymers 0.000 description 2
BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
101000993347 Gallus gallus Ciliary neurotrophic factor Proteins 0.000 description 2
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
241001494479 Pecora Species 0.000 description 2
102000007079 Peptide Fragments Human genes 0.000 description 2
108010033276 Peptide Fragments Proteins 0.000 description 2
108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 2
102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 2
108020004511 Recombinant DNA Proteins 0.000 description 2
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 2
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
235000004279 alanine Nutrition 0.000 description 2
108010011559 alanylphenylalanine Proteins 0.000 description 2
108010058966 bacteriophage T7 induced DNA polymerase Proteins 0.000 description 2
235000013405 beer Nutrition 0.000 description 2
230000008901 benefit Effects 0.000 description 2
102000005936 beta-Galactosidase Human genes 0.000 description 2
230000015572 biosynthetic process Effects 0.000 description 2
230000000295 complement effect Effects 0.000 description 2
238000002474 experimental method Methods 0.000 description 2
239000013604 expression vector Substances 0.000 description 2
239000000284 extract Substances 0.000 description 2
230000004927 fusion Effects 0.000 description 2
238000012239 gene modification Methods 0.000 description 2
230000005017 genetic modification Effects 0.000 description 2
235000013617 genetically modified food Nutrition 0.000 description 2
239000000122 growth hormone Substances 0.000 description 2
PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical compound NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 description 2
238000002372 labelling Methods 0.000 description 2
238000010369 molecular cloning Methods 0.000 description 2
230000003647 oxidation Effects 0.000 description 2
238000007254 oxidation reaction Methods 0.000 description 2
229920000642 polymer Polymers 0.000 description 2
229920001184 polypeptide Polymers 0.000 description 2
239000002244 precipitate Substances 0.000 description 2
230000008569 process Effects 0.000 description 2
102000004196 processed proteins & peptides Human genes 0.000 description 2
239000011541 reaction mixture Substances 0.000 description 2
238000002741 site-directed mutagenesis Methods 0.000 description 2
239000001632 sodium acetate Substances 0.000 description 2
235000017281 sodium acetate Nutrition 0.000 description 2
235000017557 sodium bicarbonate Nutrition 0.000 description 2
229910000030 sodium bicarbonate Inorganic materials 0.000 description 2
239000011550 stock solution Substances 0.000 description 2
238000010254 subcutaneous injection Methods 0.000 description 2
239000007929 subcutaneous injection Substances 0.000 description 2
238000000844 transformation Methods 0.000 description 2
238000013519 translation Methods 0.000 description 2
235000019786 weight gain Nutrition 0.000 description 2
AXFMEGAFCUULFV-BLFANLJRSA-N (2s)-2-[[(2s)-1-[(2s,3r)-2-amino-3-methylpentanoyl]pyrrolidine-2-carbonyl]amino]pentanedioic acid Chemical compound CC[C@@H](C)[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(O)=O)C(O)=O AXFMEGAFCUULFV-BLFANLJRSA-N 0.000 description 1
241000186361 Actinobacteria <class> Species 0.000 description 1
DYWZQNMGPYXVNS-SRVKXCTJSA-N Ala-Leu-Leu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O DYWZQNMGPYXVNS-SRVKXCTJSA-N 0.000 description 1
AWNAEZICPNGAJK-FXQIFTODSA-N Ala-Met-Ser Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CO)C(O)=O AWNAEZICPNGAJK-FXQIFTODSA-N 0.000 description 1
OSRZOHXQCUFIQG-FPMFFAJLSA-N Ala-Phe-Pro Chemical compound C([C@H](NC(=O)[C@@H]([NH3+])C)C(=O)N1[C@H](CCC1)C([O-])=O)C1=CC=CC=C1 OSRZOHXQCUFIQG-FPMFFAJLSA-N 0.000 description 1
AUFACLFHBAGZEN-ZLUOBGJFSA-N Ala-Ser-Cys Chemical compound N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CS)C(=O)O AUFACLFHBAGZEN-ZLUOBGJFSA-N 0.000 description 1
239000004254 Ammonium phosphate Substances 0.000 description 1
KWKQGHSSNHPGOW-BQBZGAKWSA-N Arg-Ala-Gly Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)NCC(O)=O KWKQGHSSNHPGOW-BQBZGAKWSA-N 0.000 description 1
MJINRRBEMOLJAK-DCAQKATOSA-N Arg-Lys-Asp Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CCCN=C(N)N MJINRRBEMOLJAK-DCAQKATOSA-N 0.000 description 1
OGZBJJLRKQZRHL-KJEVXHAQSA-N Arg-Thr-Tyr Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H]([C@H](O)C)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 OGZBJJLRKQZRHL-KJEVXHAQSA-N 0.000 description 1
QHUOOCKNNURZSL-IHRRRGAJSA-N Arg-Tyr-Ser Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CO)C(O)=O QHUOOCKNNURZSL-IHRRRGAJSA-N 0.000 description 1
FXGMURPOWCKNAZ-JYJNAYRXSA-N Arg-Val-Phe Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 FXGMURPOWCKNAZ-JYJNAYRXSA-N 0.000 description 1
ANAHQDPQQBDOBM-UHFFFAOYSA-N Arg-Val-Tyr Natural products CC(C)C(NC(=O)C(N)CCNC(=N)N)C(=O)NC(Cc1ccc(O)cc1)C(=O)O ANAHQDPQQBDOBM-UHFFFAOYSA-N 0.000 description 1
QEYJFBMTSMLPKZ-ZKWXMUAHSA-N Asn-Ala-Val Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(O)=O QEYJFBMTSMLPKZ-ZKWXMUAHSA-N 0.000 description 1
VBKIFHUVGLOJKT-FKZODXBYSA-N Asn-Thr Chemical compound C[C@@H]([C@@H](C(=O)O)NC(=O)[C@H](CC(=O)N)N)O VBKIFHUVGLOJKT-FKZODXBYSA-N 0.000 description 1
DWOGMPWRQQWPPF-GUBZILKMSA-N Asp-Leu-Glu Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(O)=O DWOGMPWRQQWPPF-GUBZILKMSA-N 0.000 description 1
GXHDGYOXPNQCKM-XVSYOHENSA-N Asp-Thr-Phe Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)O)NC(=O)[C@H](CC(=O)O)N)O GXHDGYOXPNQCKM-XVSYOHENSA-N 0.000 description 1
241000972773 Aulopiformes Species 0.000 description 1
241000894006 Bacteria Species 0.000 description 1
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
241000283707 Capra Species 0.000 description 1
108700010070 Codon Usage Proteins 0.000 description 1
UKVGHFORADMBEN-GUBZILKMSA-N Cys-Arg-Arg Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O UKVGHFORADMBEN-GUBZILKMSA-N 0.000 description 1
CHRCKSPMGYDLIA-SRVKXCTJSA-N Cys-Phe-Ser Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CO)C(O)=O CHRCKSPMGYDLIA-SRVKXCTJSA-N 0.000 description 1
YXQDRIRSAHTJKM-IMJSIDKUSA-N Cys-Ser Chemical compound SC[C@H](N)C(=O)N[C@@H](CO)C(O)=O YXQDRIRSAHTJKM-IMJSIDKUSA-N 0.000 description 1
FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
102000012410 DNA Ligases Human genes 0.000 description 1
108010061982 DNA Ligases Proteins 0.000 description 1
238000001712 DNA sequencing Methods 0.000 description 1
241000196324 Embryophyta Species 0.000 description 1
101100390711 Escherichia coli (strain K12) fhuA gene Proteins 0.000 description 1
241000287828 Gallus gallus Species 0.000 description 1
CUXJIASLBRJOFV-LAEOZQHASA-N Glu-Gly-Ile Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H]([C@@H](C)CC)C(O)=O CUXJIASLBRJOFV-LAEOZQHASA-N 0.000 description 1
JDUKCSSHWNIQQZ-IHRRRGAJSA-N Glu-Phe-Glu Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCC(O)=O)C(O)=O JDUKCSSHWNIQQZ-IHRRRGAJSA-N 0.000 description 1
RGJKYNUINKGPJN-RWRJDSDZSA-N Glu-Thr-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(=O)O)N RGJKYNUINKGPJN-RWRJDSDZSA-N 0.000 description 1
102000017722 Glutamine amidotransferases Human genes 0.000 description 1
108050005901 Glutamine amidotransferases Proteins 0.000 description 1
UHPAZODVFFYEEL-QWRGUYRKSA-N Gly-Leu-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)CN UHPAZODVFFYEEL-QWRGUYRKSA-N 0.000 description 1
HFPVRZWORNJRRC-UWVGGRQHSA-N Gly-Pro-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)CN HFPVRZWORNJRRC-UWVGGRQHSA-N 0.000 description 1
MYXNLWDWWOTERK-BHNWBGBOSA-N Gly-Thr-Pro Chemical compound C[C@H]([C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)CN)O MYXNLWDWWOTERK-BHNWBGBOSA-N 0.000 description 1
BPOHQCZZSFBSON-KKUMJFAQSA-N His-Leu-His Chemical compound CC(C)C[C@H](NC(=O)[C@@H](N)Cc1cnc[nH]1)C(=O)N[C@@H](Cc1cnc[nH]1)C(O)=O BPOHQCZZSFBSON-KKUMJFAQSA-N 0.000 description 1
108010000521 Human Growth Hormone Proteins 0.000 description 1
102000002265 Human Growth Hormone Human genes 0.000 description 1
239000000854 Human Growth Hormone Substances 0.000 description 1
TVYWVSJGSHQWMT-AJNGGQMLSA-N Ile-Leu-Lys Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)O)N TVYWVSJGSHQWMT-AJNGGQMLSA-N 0.000 description 1
102000000588 Interleukin-2 Human genes 0.000 description 1
108010002350 Interleukin-2 Proteins 0.000 description 1
FADYJNXDPBKVCA-UHFFFAOYSA-N L-Phenylalanyl-L-lysin Natural products NCCCCC(C(O)=O)NC(=O)C(N)CC1=CC=CC=C1 FADYJNXDPBKVCA-UHFFFAOYSA-N 0.000 description 1
GGLZPLKKBSSKCX-YFKPBYRVSA-N L-ethionine Chemical compound CCSCC[C@H](N)C(O)=O GGLZPLKKBSSKCX-YFKPBYRVSA-N 0.000 description 1
KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
YUGVQABRIJXYNQ-CIUDSAMLSA-N Leu-Ala-Ala Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(O)=O YUGVQABRIJXYNQ-CIUDSAMLSA-N 0.000 description 1
YUGVQABRIJXYNQ-UHFFFAOYSA-N Leu-Ala-Ala Natural products CC(C)CC(N)C(=O)NC(C)C(=O)NC(C)C(O)=O YUGVQABRIJXYNQ-UHFFFAOYSA-N 0.000 description 1
LSPYFSHXDAYVDI-SRVKXCTJSA-N Leu-Ala-Leu Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@H](C(O)=O)CC(C)C LSPYFSHXDAYVDI-SRVKXCTJSA-N 0.000 description 1
JUWJEAPUNARGCF-DCAQKATOSA-N Leu-Arg-Ala Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(O)=O JUWJEAPUNARGCF-DCAQKATOSA-N 0.000 description 1
UILIPCLTHRPCRB-XUXIUFHCSA-N Leu-Arg-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(C)C)N UILIPCLTHRPCRB-XUXIUFHCSA-N 0.000 description 1
HFBCHNRFRYLZNV-GUBZILKMSA-N Leu-Glu-Asp Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O HFBCHNRFRYLZNV-GUBZILKMSA-N 0.000 description 1
QVFGXCVIXXBFHO-AVGNSLFASA-N Leu-Glu-Leu Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(O)=O QVFGXCVIXXBFHO-AVGNSLFASA-N 0.000 description 1
KVOFSTUWVSQMDK-KKUMJFAQSA-N Leu-His-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC(C)C)CC1=CN=CN1 KVOFSTUWVSQMDK-KKUMJFAQSA-N 0.000 description 1
ZDBMWELMUCLUPL-QEJZJMRPSA-N Leu-Phe-Ala Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(=O)N[C@@H](C)C(O)=O)CC1=CC=CC=C1 ZDBMWELMUCLUPL-QEJZJMRPSA-N 0.000 description 1
RGUXWMDNCPMQFB-YUMQZZPRSA-N Leu-Ser-Gly Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CO)C(=O)NCC(O)=O RGUXWMDNCPMQFB-YUMQZZPRSA-N 0.000 description 1
XOEDPXDZJHBQIX-ULQDDVLXSA-N Leu-Val-Phe Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 XOEDPXDZJHBQIX-ULQDDVLXSA-N 0.000 description 1
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
102000003960 Ligases Human genes 0.000 description 1
108090000364 Ligases Proteins 0.000 description 1
QYOXSYXPHUHOJR-GUBZILKMSA-N Lys-Asn-Glu Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O QYOXSYXPHUHOJR-GUBZILKMSA-N 0.000 description 1
PXHCFKXNSBJSTQ-KKUMJFAQSA-N Lys-Asn-Tyr Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CCCCN)N)O PXHCFKXNSBJSTQ-KKUMJFAQSA-N 0.000 description 1
RBEATVHTWHTHTJ-KKUMJFAQSA-N Lys-Leu-Lys Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(O)=O RBEATVHTWHTHTJ-KKUMJFAQSA-N 0.000 description 1
TWPCWKVOZDUYAA-KKUMJFAQSA-N Lys-Phe-Asp Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC(O)=O)C(O)=O TWPCWKVOZDUYAA-KKUMJFAQSA-N 0.000 description 1
MGKFCQFVPKOWOL-CIUDSAMLSA-N Lys-Ser-Asp Chemical compound C(CCN)C[C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)O)C(=O)O)N MGKFCQFVPKOWOL-CIUDSAMLSA-N 0.000 description 1
229930195725 Mannitol Natural products 0.000 description 1
CTVJSFRHUOSCQQ-DCAQKATOSA-N Met-Arg-Glu Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(O)=O CTVJSFRHUOSCQQ-DCAQKATOSA-N 0.000 description 1
102000016943 Muramidase Human genes 0.000 description 1
108010014251 Muramidase Proteins 0.000 description 1
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
YBAFDPFAUTYYRW-UHFFFAOYSA-N N-L-alpha-glutamyl-L-leucine Natural products CC(C)CC(C(O)=O)NC(=O)C(N)CCC(O)=O YBAFDPFAUTYYRW-UHFFFAOYSA-N 0.000 description 1
241000364057 Peoria Species 0.000 description 1
ZLGQEBCCANLYRA-RYUDHWBXSA-N Phe-Gly-Glu Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(O)=O ZLGQEBCCANLYRA-RYUDHWBXSA-N 0.000 description 1
YCCUXNNKXDGMAM-KKUMJFAQSA-N Phe-Leu-Ser Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(O)=O YCCUXNNKXDGMAM-KKUMJFAQSA-N 0.000 description 1
DCHQYSOGURGJST-FJXKBIBVSA-N Pro-Thr-Gly Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(O)=O DCHQYSOGURGJST-FJXKBIBVSA-N 0.000 description 1
101100145480 Prochlorococcus marinus (strain SARG / CCMP1375 / SS120) rpoC2 gene Proteins 0.000 description 1
108010003201 RGH 0205 Proteins 0.000 description 1
108010025216 RVF peptide Proteins 0.000 description 1
240000004808 Saccharomyces cerevisiae Species 0.000 description 1
238000012300 Sequence Analysis Methods 0.000 description 1
CNIIKZQXBBQHCX-FXQIFTODSA-N Ser-Asp-Arg Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O CNIIKZQXBBQHCX-FXQIFTODSA-N 0.000 description 1
MESDJCNHLZBMEP-ZLUOBGJFSA-N Ser-Asp-Asp Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O MESDJCNHLZBMEP-ZLUOBGJFSA-N 0.000 description 1
XSYJDGIDKRNWFX-SRVKXCTJSA-N Ser-Cys-Phe Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O XSYJDGIDKRNWFX-SRVKXCTJSA-N 0.000 description 1
VMLONWHIORGALA-SRVKXCTJSA-N Ser-Leu-Leu Chemical compound CC(C)C[C@@H](C([O-])=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H]([NH3+])CO VMLONWHIORGALA-SRVKXCTJSA-N 0.000 description 1
FVFUOQIYDPAIJR-XIRDDKMYSA-N Ser-Trp-Leu Chemical compound CC(C)C[C@@H](C(=O)O)NC(=O)[C@H](CC1=CNC2=CC=CC=C21)NC(=O)[C@H](CO)N FVFUOQIYDPAIJR-XIRDDKMYSA-N 0.000 description 1
UIIMBOGNXHQVGW-DEQYMQKBSA-M Sodium bicarbonate-14C Chemical compound [Na+].O[14C]([O-])=O UIIMBOGNXHQVGW-DEQYMQKBSA-M 0.000 description 1
108700005078 Synthetic Genes Proteins 0.000 description 1
101150104425 T4 gene Proteins 0.000 description 1
108020005038 Terminator Codon Proteins 0.000 description 1
QNJZOAHSYPXTAB-VEVYYDQMSA-N Thr-Asn-Met Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCSC)C(O)=O QNJZOAHSYPXTAB-VEVYYDQMSA-N 0.000 description 1
OJRNZRROAIAHDL-LKXGYXEUSA-N Thr-Asn-Ser Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(O)=O OJRNZRROAIAHDL-LKXGYXEUSA-N 0.000 description 1
XOTBWOCSLMBGMF-SUSMZKCASA-N Thr-Glu-Thr Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O XOTBWOCSLMBGMF-SUSMZKCASA-N 0.000 description 1
BZTSQFWJNJYZSX-JRQIVUDYSA-N Thr-Tyr-Asp Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(O)=O)C(O)=O BZTSQFWJNJYZSX-JRQIVUDYSA-N 0.000 description 1
239000007984 Tris EDTA buffer Substances 0.000 description 1
QSFJHIRIHOJRKS-ULQDDVLXSA-N Tyr-Leu-Arg Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O QSFJHIRIHOJRKS-ULQDDVLXSA-N 0.000 description 1
JFAWZADYPRMRCO-UBHSHLNASA-N Val-Ala-Phe Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 JFAWZADYPRMRCO-UBHSHLNASA-N 0.000 description 1
UEPLNXPLHJUYPT-AVGNSLFASA-N Val-Met-Lys Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(O)=O UEPLNXPLHJUYPT-AVGNSLFASA-N 0.000 description 1
PFMSJVIPEZMKSC-DZKIICNBSA-N Val-Tyr-Glu Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)N[C@@H](CCC(=O)O)C(=O)O)N PFMSJVIPEZMKSC-DZKIICNBSA-N 0.000 description 1
KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
241001672648 Vieira Species 0.000 description 1
239000002253 acid Substances 0.000 description 1
239000011543 agarose gel Substances 0.000 description 1
108010041407 alanylaspartic acid Proteins 0.000 description 1
230000002152 alkylating effect Effects 0.000 description 1
230000029936 alkylation Effects 0.000 description 1
238000005804 alkylation reaction Methods 0.000 description 1
KOSRFJWDECSPRO-UHFFFAOYSA-N alpha-L-glutamyl-L-glutamic acid Natural products OC(=O)CCC(N)C(=O)NC(CCC(O)=O)C(O)=O KOSRFJWDECSPRO-UHFFFAOYSA-N 0.000 description 1
230000004075 alteration Effects 0.000 description 1
150000001408 amides Chemical class 0.000 description 1
229910000148 ammonium phosphate Inorganic materials 0.000 description 1
235000019289 ammonium phosphates Nutrition 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
238000005571 anion exchange chromatography Methods 0.000 description 1
238000000137 annealing Methods 0.000 description 1
230000000890 antigenic effect Effects 0.000 description 1
239000008346 aqueous phase Substances 0.000 description 1
108010036533 arginylvaline Proteins 0.000 description 1
108010092854 aspartyllysine Proteins 0.000 description 1
238000003556 assay Methods 0.000 description 1
239000013584 assay control Substances 0.000 description 1
230000000903 blocking effect Effects 0.000 description 1
238000009835 boiling Methods 0.000 description 1
244000309464 bull Species 0.000 description 1
239000001110 calcium chloride Substances 0.000 description 1
229910001628 calcium chloride Inorganic materials 0.000 description 1
235000011148 calcium chloride Nutrition 0.000 description 1
229940041514 candida albicans extract Drugs 0.000 description 1
238000004113 cell culture Methods 0.000 description 1
230000001413 cellular effect Effects 0.000 description 1
238000007385 chemical modification Methods 0.000 description 1
239000003153 chemical reaction reagent Substances 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
235000013330 chicken meat Nutrition 0.000 description 1
238000004587 chromatography analysis Methods 0.000 description 1
239000003593 chromogenic compound Substances 0.000 description 1
230000002759 chromosomal effect Effects 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
235000020247 cow milk Nutrition 0.000 description 1
HAAZLUGHYHWQIW-KVQBGUIXSA-N dGTP Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 HAAZLUGHYHWQIW-KVQBGUIXSA-N 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
MNNHAPBLZZVQHP-UHFFFAOYSA-N diammonium hydrogen phosphate Chemical compound [NH4+].[NH4+].OP([O-])([O-])=O MNNHAPBLZZVQHP-UHFFFAOYSA-N 0.000 description 1
239000000539 dimer Substances 0.000 description 1
201000010099 disease Diseases 0.000 description 1
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
239000003814 drug Substances 0.000 description 1
229940079593 drug Drugs 0.000 description 1
239000002158 endotoxin Substances 0.000 description 1
239000013613 expression plasmid Substances 0.000 description 1
238000000855 fermentation Methods 0.000 description 1
230000004151 fermentation Effects 0.000 description 1
101150041954 galU gene Proteins 0.000 description 1
230000002068 genetic effect Effects 0.000 description 1
102000034238 globular proteins Human genes 0.000 description 1
108091005896 globular proteins Proteins 0.000 description 1
ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
108010042598 glutamyl-aspartyl-glycine Proteins 0.000 description 1
108010055341 glutamyl-glutamic acid Proteins 0.000 description 1
108010049041 glutamylalanine Proteins 0.000 description 1
108010066198 glycyl-leucyl-phenylalanine Proteins 0.000 description 1
108010089804 glycyl-threonine Proteins 0.000 description 1
239000007952 growth promoter Substances 0.000 description 1
101150096208 gtaB gene Proteins 0.000 description 1
238000010438 heat treatment Methods 0.000 description 1
244000309465 heifer Species 0.000 description 1
239000008241 heterogeneous mixture Substances 0.000 description 1
239000005556 hormone Substances 0.000 description 1
229940088597 hormone Drugs 0.000 description 1
238000000338 in vitro Methods 0.000 description 1
238000001727 in vivo Methods 0.000 description 1
210000003000 inclusion body Anatomy 0.000 description 1
238000011534 incubation Methods 0.000 description 1
230000001939 inductive effect Effects 0.000 description 1
230000000977 initiatory effect Effects 0.000 description 1
239000007927 intramuscular injection Substances 0.000 description 1
238000010255 intramuscular injection Methods 0.000 description 1
JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 1
238000005342 ion exchange Methods 0.000 description 1
125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
108010049589 leucyl-leucyl-leucine Proteins 0.000 description 1
108010091871 leucylmethionine Proteins 0.000 description 1
239000008176 lyophilized powder Substances 0.000 description 1
239000006166 lysate Substances 0.000 description 1
229960000274 lysozyme Drugs 0.000 description 1
239000004325 lysozyme Substances 0.000 description 1
235000010335 lysozyme Nutrition 0.000 description 1
230000014759 maintenance of location Effects 0.000 description 1
239000000594 mannitol Substances 0.000 description 1
235000010355 mannitol Nutrition 0.000 description 1
208000004396 mastitis Diseases 0.000 description 1
235000013372 meat Nutrition 0.000 description 1
208000030159 metabolic disease Diseases 0.000 description 1
210000003205 muscle Anatomy 0.000 description 1
238000002703 mutagenesis Methods 0.000 description 1
231100000350 mutagenesis Toxicity 0.000 description 1
210000004897 n-terminal region Anatomy 0.000 description 1
108020004707 nucleic acids Proteins 0.000 description 1
102000039446 nucleic acids Human genes 0.000 description 1
150000007523 nucleic acids Chemical class 0.000 description 1
210000004738 parenchymal cell Anatomy 0.000 description 1
239000012071 phase Substances 0.000 description 1
COLNVLDHVKWLRT-QMMMGPOBSA-N phenylalanine group Chemical group N[C@@H](CC1=CC=CC=C1)C(=O)O COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
230000026731 phosphorylation Effects 0.000 description 1
238000006366 phosphorylation reaction Methods 0.000 description 1
235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
229920000053 polysorbate 80 Polymers 0.000 description 1
230000004481 post-translational protein modification Effects 0.000 description 1
238000004886 process control Methods 0.000 description 1
108010004914 prolylarginine Proteins 0.000 description 1
239000013636 protein dimer Substances 0.000 description 1
101150002764 purA gene Proteins 0.000 description 1
238000000746 purification Methods 0.000 description 1
230000009467 reduction Effects 0.000 description 1
108091008146 restriction endonucleases Proteins 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
238000004007 reversed phase HPLC Methods 0.000 description 1
210000003705 ribosome Anatomy 0.000 description 1
101150109946 rpo1C gene Proteins 0.000 description 1
101150095619 rpoBC gene Proteins 0.000 description 1
101150042391 rpoC gene Proteins 0.000 description 1
101150103066 rpoC1 gene Proteins 0.000 description 1
235000019515 salmon Nutrition 0.000 description 1
230000007017 scission Effects 0.000 description 1
239000001488 sodium phosphate Substances 0.000 description 1
229910000162 sodium phosphate Inorganic materials 0.000 description 1
235000011008 sodium phosphates Nutrition 0.000 description 1
238000012453 sprague-dawley rat model Methods 0.000 description 1
238000003756 stirring Methods 0.000 description 1
239000000126 substance Substances 0.000 description 1
125000003396 thiol group Chemical group [H]S* 0.000 description 1
210000002303 tibia Anatomy 0.000 description 1
238000013518 transcription Methods 0.000 description 1
230000035897 transcription Effects 0.000 description 1
230000002103 transcriptional effect Effects 0.000 description 1
230000009261 transgenic effect Effects 0.000 description 1
RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
239000004474 valine Substances 0.000 description 1
239000012138 yeast extract Substances 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
- 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

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Endocrinology (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
Genetics & Genomics (AREA)
Toxicology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Zoology (AREA)
Medicinal Chemistry (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Gastroenterology & Hepatology (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Cosmetics (AREA)
Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Fodder In General (AREA)

AU46631/89A 1989-01-31 1989-12-11 Somatotropin analogs Ceased AU620673B2 (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US30473389A	1989-01-31	1989-01-31
US304733		1989-01-31

Publications (2)

Publication Number	Publication Date
AU4663189A AU4663189A (en)	1990-08-24
AU620673B2 true AU620673B2 (en)	1992-02-20

Family

ID=23177749

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
AU46631/89A Ceased AU620673B2 (en)	1989-01-31	1989-12-11	Somatotropin analogs

Country Status (6)

Country	Link
EP (1)	EP0456642A1 (ja)
JP (1)	JP3207416B2 (ja)
AU (1)	AU620673B2 (ja)
CA (1)	CA2005502C (ja)
DK (1)	DK140491A (ja)
WO (1)	WO1990008823A1 (ja)

Families Citing this family (32)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP0355460B1 (en) *	1988-08-24	2000-12-27	American Cyanamid Company	Stabilization of somatotropins by modification of cysteine residues utilizing site directed mutagenesis or chemical derivatization
US5688666A (en) *	1988-10-28	1997-11-18	Genentech, Inc.	Growth hormone variants with altered binding properties
US5534617A (en) *	1988-10-28	1996-07-09	Genentech, Inc.	Human growth hormone variants having greater affinity for human growth hormone receptor at site 1
US5849694A (en) *	1990-07-16	1998-12-15	Synenki; Richard M.	Stable and bioactive modified porcine somatotropin and pharmaceutical compositions thereof
DK0851925T3 (da) *	1995-09-21	2005-11-28	Genentech Inc	Humane Væksthormonvarianter
US8008252B2 (en)	2001-10-10	2011-08-30	Novo Nordisk A/S	Factor VII: remodeling and glycoconjugation of Factor VII
US7696163B2 (en)	2001-10-10	2010-04-13	Novo Nordisk A/S	Erythropoietin: remodeling and glycoconjugation of erythropoietin
US7173003B2 (en)	2001-10-10	2007-02-06	Neose Technologies, Inc.	Granulocyte colony stimulating factor: remodeling and glycoconjugation of G-CSF
US7214660B2 (en)	2001-10-10	2007-05-08	Neose Technologies, Inc.	Erythropoietin: remodeling and glycoconjugation of erythropoietin
US7795210B2 (en)	2001-10-10	2010-09-14	Novo Nordisk A/S	Protein remodeling methods and proteins/peptides produced by the methods
NZ542094A (en)	2003-03-14	2008-12-24	Neose Technologies Inc	Branched polymer conjugates comprising a peptide and water-soluble polymer chains
PL1615945T3 (pl)	2003-04-09	2012-03-30	Ratiopharm Gmbh	Sposoby glikopegylacji i białka/peptydy wytwarzane tymi sposobami
JP2007523630A (ja) *	2003-05-09	2007-08-23	ネオステクノロジーズインコーポレイテッド	ヒト成長ホルモングリコシル化突然変異体の組成と調合法
US9005625B2 (en)	2003-07-25	2015-04-14	Novo Nordisk A/S	Antibody toxin conjugates
US8633157B2 (en)	2003-11-24	2014-01-21	Novo Nordisk A/S	Glycopegylated erythropoietin
US7842661B2 (en)	2003-11-24	2010-11-30	Novo Nordisk A/S	Glycopegylated erythropoietin formulations
US20080305992A1 (en)	2003-11-24	2008-12-11	Neose Technologies, Inc.	Glycopegylated erythropoietin
US7956032B2 (en)	2003-12-03	2011-06-07	Novo Nordisk A/S	Glycopegylated granulocyte colony stimulating factor
NZ548123A (en)	2004-01-08	2010-05-28	Novo Nordisk As	O-linked glycosylation of peptides
US20080300173A1 (en)	2004-07-13	2008-12-04	Defrees Shawn	Branched Peg Remodeling and Glycosylation of Glucagon-Like Peptides-1 [Glp-1]
WO2006031811A2 (en)	2004-09-10	2006-03-23	Neose Technologies, Inc.	Glycopegylated interferon alpha
WO2006050247A2 (en)	2004-10-29	2006-05-11	Neose Technologies, Inc.	Remodeling and glycopegylation of fibroblast growth factor (fgf)
US9029331B2 (en)	2005-01-10	2015-05-12	Novo Nordisk A/S	Glycopegylated granulocyte colony stimulating factor
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
US20070105755A1 (en)	2005-10-26	2007-05-10	Neose Technologies, Inc.	One pot desialylation and glycopegylation of therapeutic peptides
WO2007056191A2 (en)	2005-11-03	2007-05-18	Neose Technologies, Inc.	Nucleotide sugar purification using membranes
EP2049144B8 (en)	2006-07-21	2015-02-18	ratiopharm GmbH	Glycosylation of peptides via o-linked glycosylation sequences
EP2054521A4 (en)	2006-10-03	2012-12-19	Novo Nordisk As	PROCESS FOR CLEANING POLYPEPTIDE CONJUGATES
HRP20130382T1 (hr)	2007-04-03	2013-05-31	Biogenerix Ag	Postupci lijeäśenja pomoä†u glikopegiliranog g-csf
CA2690611C (en)	2007-06-12	2015-12-08	Novo Nordisk A/S	Improved process for the production of nucleotide sugars
US8207112B2 (en)	2007-08-29	2012-06-26	Biogenerix Ag	Liquid formulation of G-CSF conjugate
PL2257311T3 (pl)	2008-02-27	2014-09-30	Novo Nordisk As	Koniugaty cząsteczek czynnika VIII

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
IE56026B1 (en) *	1982-10-19	1991-03-27	Cetus Corp	Cysteine-depleted muteins of biologically active proteins

1989
- 1989-12-11 JP JP50136890A patent/JP3207416B2/ja not_active Expired - Fee Related
- 1989-12-11 AU AU46631/89A patent/AU620673B2/en not_active Ceased
- 1989-12-11 WO PCT/US1989/005445 patent/WO1990008823A1/en not_active Ceased
- 1989-12-11 EP EP19900901301 patent/EP0456642A1/en not_active Withdrawn
- 1989-12-15 CA CA 2005502 patent/CA2005502C/en not_active Expired - Fee Related
1991
- 1991-07-29 DK DK140491A patent/DK140491A/da not_active Application Discontinuation

Also Published As

Publication number	Publication date
AU4663189A (en)	1990-08-24
JP3207416B2 (ja)	2001-09-10
DK140491D0 (da)	1991-07-29
DK140491A (da)	1991-07-29
CA2005502C (en)	2001-06-05
EP0456642A1 (en)	1991-11-21
CA2005502A1 (en)	1990-07-31
WO1990008823A1 (en)	1990-08-09
JPH04503001A (ja)	1992-06-04

Legal Events

Date	Code	Title	Description
2003-07-10	MK14	Patent ceased section 143(a) (annual fees not paid) or expired

Publication	Publication Date	Title
AU620673B2 (en)	1992-02-20	Somatotropin analogs
JP2583214B2 (ja)	1997-02-19	牛ソマトトロピン含有組成物およびこれを用いる牛の乳汁分秘促進法
AU634517B2 (en)	1993-02-25	Somatotropin analogs
US4861868A (en)	1989-08-29	Production of proteins in procaryotes
CZ636081A3 (en)	1995-02-15	Process for preparing a vector for dna transfer
US5605815A (en)	1997-02-25	Nucleic acids encoding and expression of parathyroid hormone-like peptide
RU2034457C1 (ru)	1995-05-10	Способ повышения продуктивности сельскохозяйственных животных и препарат для его осуществления
US5141922A (en)	1992-08-25	Biologically active proteins and a method for their use
US5631227A (en)	1997-05-20	Somatotropin analogs
EP0236452B1 (en)	1990-10-31	Enhanced bioactivity of mammalian somatotropin through selective deamidation
JP2619036B2 (ja)	1997-06-11	ブタ成長ホルモンアナログ
AU633278B2 (en)	1993-01-28	Isolation and cloning of complementary dna for gene coding of bovine trophoblast protein-1
EP0263206B1 (en)	1990-12-12	Enhanced bioactivity of mammalian somatotropin through selective deamidation
Hanks et al.	1989	Expression of biologically active recombinant-derived chicken prolactin in Escherichia coli
EP0363063A2 (en)	1990-04-11	Sheep growth hormone
AU647374B2 (en)	1994-03-24	Sheep growth hormone
JP2666069B2 (ja)	1997-10-22	組換え型鳥類プロラクチン又は組換え型鳥類プレプロラクチン，組換え型ニワトリプロラクチン，組換え型ニワトリプロラクチン構造遺伝子，組換え型ニワトリプレプロラクチン，組換え型ニワトリプレプロラクチン構造遺伝子，組換えプラスミド，組換えプラスミドを含む微生物
JPH02219576A (ja)	1990-09-03	魚類成長ホルモン遺伝子