NO317394B1 - Enkelt-kjede former av glykoprotein-hormon-kvartetten - Google Patents
Enkelt-kjede former av glykoprotein-hormon-kvartetten Download PDFInfo
- Publication number
- NO317394B1 NO317394B1 NO19961433A NO961433A NO317394B1 NO 317394 B1 NO317394 B1 NO 317394B1 NO 19961433 A NO19961433 A NO 19961433A NO 961433 A NO961433 A NO 961433A NO 317394 B1 NO317394 B1 NO 317394B1
- Authority
- NO
- Norway
- Prior art keywords
- ctp
- subunit
- agonist
- antagonist
- linker
- Prior art date
Links
- 229940088597 hormone Drugs 0.000 title claims abstract description 82
- 239000005556 hormone Substances 0.000 title claims abstract description 82
- 239000005557 antagonist Substances 0.000 claims abstract description 37
- 102000003886 Glycoproteins Human genes 0.000 claims abstract description 32
- 108090000288 Glycoproteins Proteins 0.000 claims abstract description 32
- 239000000556 agonist Substances 0.000 claims abstract description 31
- 230000003054 hormonal effect Effects 0.000 claims abstract description 9
- 101800005309 Carboxy-terminal peptide Proteins 0.000 claims description 88
- 108090000623 proteins and genes Proteins 0.000 claims description 67
- 102000004169 proteins and genes Human genes 0.000 claims description 55
- 150000001413 amino acids Chemical class 0.000 claims description 49
- 230000000694 effects Effects 0.000 claims description 44
- 102000011022 Chorionic Gonadotropin Human genes 0.000 claims description 40
- 108010062540 Chorionic Gonadotropin Proteins 0.000 claims description 40
- 238000006467 substitution reaction Methods 0.000 claims description 31
- 238000000034 method Methods 0.000 claims description 30
- 210000004027 cell Anatomy 0.000 claims description 29
- 102000012673 Follicle Stimulating Hormone Human genes 0.000 claims description 25
- 108010079345 Follicle Stimulating Hormone Proteins 0.000 claims description 25
- 229940028334 follicle stimulating hormone Drugs 0.000 claims description 25
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 24
- 210000004899 c-terminal region Anatomy 0.000 claims description 21
- 229940015047 chorionic gonadotropin Drugs 0.000 claims description 20
- 229940084986 human chorionic gonadotropin Drugs 0.000 claims description 20
- 102000009151 Luteinizing Hormone Human genes 0.000 claims description 16
- 108010073521 Luteinizing Hormone Proteins 0.000 claims description 16
- 229940040129 luteinizing hormone Drugs 0.000 claims description 16
- 102000011923 Thyrotropin Human genes 0.000 claims description 13
- 108010061174 Thyrotropin Proteins 0.000 claims description 13
- 238000004519 manufacturing process Methods 0.000 claims description 13
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 9
- 238000003780 insertion Methods 0.000 claims description 8
- 230000037431 insertion Effects 0.000 claims description 8
- 239000002773 nucleotide Substances 0.000 claims description 8
- 125000003729 nucleotide group Chemical group 0.000 claims description 8
- 238000012217 deletion Methods 0.000 claims description 6
- 230000037430 deletion Effects 0.000 claims description 6
- 238000011144 upstream manufacturing Methods 0.000 claims description 6
- 230000036961 partial effect Effects 0.000 claims description 5
- 125000000539 amino acid group Chemical group 0.000 claims description 4
- 102000035122 glycosylated proteins Human genes 0.000 claims description 2
- 108091005608 glycosylated proteins Proteins 0.000 claims description 2
- 230000002452 interceptive effect Effects 0.000 claims description 2
- 238000011084 recovery Methods 0.000 claims description 2
- 239000000203 mixture Substances 0.000 claims 2
- 239000000546 pharmaceutical excipient Substances 0.000 claims 1
- 229940124531 pharmaceutical excipient Drugs 0.000 claims 1
- 125000005647 linker group Chemical group 0.000 abstract description 51
- 239000003814 drug Substances 0.000 abstract description 15
- 229940079593 drug Drugs 0.000 abstract description 14
- 150000001875 compounds Chemical class 0.000 abstract description 12
- 241000251539 Vertebrata <Metazoa> Species 0.000 abstract description 6
- 235000001014 amino acid Nutrition 0.000 description 53
- 235000018102 proteins Nutrition 0.000 description 49
- 229940024606 amino acid Drugs 0.000 description 48
- 108090000765 processed proteins & peptides Proteins 0.000 description 30
- 230000013595 glycosylation Effects 0.000 description 29
- 238000006206 glycosylation reaction Methods 0.000 description 29
- 108020003175 receptors Proteins 0.000 description 19
- 102000005962 receptors Human genes 0.000 description 19
- 239000000463 material Substances 0.000 description 16
- 230000007935 neutral effect Effects 0.000 description 16
- 239000000833 heterodimer Substances 0.000 description 13
- 125000003118 aryl group Chemical group 0.000 description 11
- 238000010276 construction Methods 0.000 description 10
- 230000027455 binding Effects 0.000 description 9
- 238000006243 chemical reaction Methods 0.000 description 9
- 230000007717 exclusion Effects 0.000 description 9
- 239000013604 expression vector Substances 0.000 description 9
- 238000002372 labelling Methods 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- 108020004414 DNA Proteins 0.000 description 8
- 230000015572 biosynthetic process Effects 0.000 description 8
- 239000000539 dimer Substances 0.000 description 8
- 239000012634 fragment Substances 0.000 description 8
- 230000004048 modification Effects 0.000 description 8
- 238000012986 modification Methods 0.000 description 8
- 102100031196 Choriogonadotropin subunit beta 3 Human genes 0.000 description 7
- 108091026890 Coding region Proteins 0.000 description 7
- 108020004705 Codon Proteins 0.000 description 7
- 238000004458 analytical method Methods 0.000 description 7
- 102000004196 processed proteins & peptides Human genes 0.000 description 7
- 108700024394 Exon Proteins 0.000 description 6
- KSPIYJQBLVDRRI-UHFFFAOYSA-N N-methylisoleucine Chemical compound CCC(C)C(NC)C(O)=O KSPIYJQBLVDRRI-UHFFFAOYSA-N 0.000 description 6
- 230000004989 O-glycosylation Effects 0.000 description 6
- 239000000969 carrier Substances 0.000 description 6
- 241000282412 Homo Species 0.000 description 5
- 239000012736 aqueous medium Substances 0.000 description 5
- 230000000875 corresponding effect Effects 0.000 description 5
- 125000004122 cyclic group Chemical group 0.000 description 5
- FUOOLUPWFVMBKG-UHFFFAOYSA-N 2-Aminoisobutyric acid Chemical compound CC(C)(N)C(O)=O FUOOLUPWFVMBKG-UHFFFAOYSA-N 0.000 description 4
- 230000004988 N-glycosylation Effects 0.000 description 4
- 239000007864 aqueous solution Substances 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- UCMIRNVEIXFBKS-UHFFFAOYSA-N beta-alanine Chemical compound NCCC(O)=O UCMIRNVEIXFBKS-UHFFFAOYSA-N 0.000 description 4
- 230000004071 biological effect Effects 0.000 description 4
- 239000003153 chemical reaction reagent Substances 0.000 description 4
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 description 4
- 238000010647 peptide synthesis reaction Methods 0.000 description 4
- 238000003752 polymerase chain reaction Methods 0.000 description 4
- 230000001105 regulatory effect Effects 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- MRTPISKDZDHEQI-YFKPBYRVSA-N (2s)-2-(tert-butylamino)propanoic acid Chemical compound OC(=O)[C@H](C)NC(C)(C)C MRTPISKDZDHEQI-YFKPBYRVSA-N 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 102000008175 FSH Receptors Human genes 0.000 description 3
- 108010060374 FSH Receptors Proteins 0.000 description 3
- 108010002386 Interleukin-3 Proteins 0.000 description 3
- 102000000646 Interleukin-3 Human genes 0.000 description 3
- 108091092195 Intron Proteins 0.000 description 3
- QEFRNWWLZKMPFJ-ZXPFJRLXSA-N L-methionine (R)-S-oxide Chemical compound C[S@@](=O)CC[C@H]([NH3+])C([O-])=O QEFRNWWLZKMPFJ-ZXPFJRLXSA-N 0.000 description 3
- QEFRNWWLZKMPFJ-UHFFFAOYSA-N L-methionine sulphoxide Natural products CS(=O)CCC(N)C(O)=O QEFRNWWLZKMPFJ-UHFFFAOYSA-N 0.000 description 3
- 102000023108 LH Receptors Human genes 0.000 description 3
- 108010011942 LH Receptors Proteins 0.000 description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 239000004472 Lysine Substances 0.000 description 3
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 3
- 230000002378 acidificating effect Effects 0.000 description 3
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 3
- 125000003277 amino group Chemical group 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- 238000010168 coupling process Methods 0.000 description 3
- 239000013078 crystal Substances 0.000 description 3
- 229960003067 cystine Drugs 0.000 description 3
- 238000013461 design Methods 0.000 description 3
- 238000003018 immunoassay Methods 0.000 description 3
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 3
- 229960000310 isoleucine Drugs 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 238000003259 recombinant expression Methods 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 3
- 230000019491 signal transduction Effects 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 102000003390 tumor necrosis factor Human genes 0.000 description 3
- NPDBDJFLKKQMCM-SCSAIBSYSA-N (2s)-2-amino-3,3-dimethylbutanoic acid Chemical compound CC(C)(C)[C@H](N)C(O)=O NPDBDJFLKKQMCM-SCSAIBSYSA-N 0.000 description 2
- IMGGANUNCHXAQF-UHFFFAOYSA-N 2-sulfanylpentanoic acid Chemical compound CCCC(S)C(O)=O IMGGANUNCHXAQF-UHFFFAOYSA-N 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 241000283073 Equus caballus Species 0.000 description 2
- 102100040977 Follitropin subunit beta Human genes 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 102000006771 Gonadotropins Human genes 0.000 description 2
- 108010086677 Gonadotropins Proteins 0.000 description 2
- 108010065805 Interleukin-12 Proteins 0.000 description 2
- 102000013462 Interleukin-12 Human genes 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
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- 108050004114 Monellin Proteins 0.000 description 2
- 241000276498 Pollachius virens Species 0.000 description 2
- 241000288906 Primates Species 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- 102000009618 Transforming Growth Factors Human genes 0.000 description 2
- 108010009583 Transforming Growth Factors Proteins 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
- 238000012875 competitive assay Methods 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- XVOYSCVBGLVSOL-UHFFFAOYSA-N cysteic acid Chemical compound OC(=O)C(N)CS(O)(=O)=O XVOYSCVBGLVSOL-UHFFFAOYSA-N 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- 150000004985 diamines Chemical class 0.000 description 2
- 150000001990 dicarboxylic acid derivatives Chemical class 0.000 description 2
- 150000002009 diols Chemical class 0.000 description 2
- 239000007850 fluorescent dye Substances 0.000 description 2
- 238000001215 fluorescent labelling Methods 0.000 description 2
- 229960003692 gamma aminobutyric acid Drugs 0.000 description 2
- 235000013922 glutamic acid Nutrition 0.000 description 2
- 239000004220 glutamic acid Substances 0.000 description 2
- 239000002622 gonadotropin Substances 0.000 description 2
- 229940094892 gonadotropins Drugs 0.000 description 2
- GPRLSGONYQIRFK-UHFFFAOYSA-N hydron Chemical compound [H+] GPRLSGONYQIRFK-UHFFFAOYSA-N 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- 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 2
- 230000003993 interaction Effects 0.000 description 2
- 125000000741 isoleucyl group Chemical group [H]N([H])C(C(C([H])([H])[H])C([H])([H])C([H])([H])[H])C(=O)O* 0.000 description 2
- 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 2
- 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 2
- 229930182817 methionine Natural products 0.000 description 2
- 239000008194 pharmaceutical composition Substances 0.000 description 2
- 230000001323 posttranslational effect Effects 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 2
- 238000010188 recombinant method Methods 0.000 description 2
- FSYKKLYZXJSNPZ-UHFFFAOYSA-N sarcosine Chemical compound C[NH2+]CC([O-])=O FSYKKLYZXJSNPZ-UHFFFAOYSA-N 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 230000008054 signal transmission Effects 0.000 description 2
- 238000002741 site-directed mutagenesis Methods 0.000 description 2
- 239000007790 solid phase Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- BVAUMRCGVHUWOZ-ZETCQYMHSA-N (2s)-2-(cyclohexylazaniumyl)propanoate Chemical compound OC(=O)[C@H](C)NC1CCCCC1 BVAUMRCGVHUWOZ-ZETCQYMHSA-N 0.000 description 1
- RWLSBXBFZHDHHX-VIFPVBQESA-N (2s)-2-(naphthalen-2-ylamino)propanoic acid Chemical compound C1=CC=CC2=CC(N[C@@H](C)C(O)=O)=CC=C21 RWLSBXBFZHDHHX-VIFPVBQESA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- PNDPGZBMCMUPRI-HVTJNCQCSA-N 10043-66-0 Chemical compound [131I][131I] PNDPGZBMCMUPRI-HVTJNCQCSA-N 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 101710116299 Choriogonadotropin subunit beta Proteins 0.000 description 1
- 101710166590 Choriogonadotropin subunit beta 3 Proteins 0.000 description 1
- 102000007644 Colony-Stimulating Factors Human genes 0.000 description 1
- 108010071942 Colony-Stimulating Factors Proteins 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 102000018386 EGF Family of Proteins Human genes 0.000 description 1
- 108010066486 EGF Family of Proteins Proteins 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 102000018233 Fibroblast Growth Factor Human genes 0.000 description 1
- 108050007372 Fibroblast Growth Factor Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000893054 Homo sapiens Follitropin subunit beta Proteins 0.000 description 1
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 108010002350 Interleukin-2 Proteins 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- AHLPHDHHMVZTML-BYPYZUCNSA-N L-Ornithine Chemical compound NCCC[C@H](N)C(O)=O AHLPHDHHMVZTML-BYPYZUCNSA-N 0.000 description 1
- ZGUNAGUHMKGQNY-ZETCQYMHSA-N L-alpha-phenylglycine zwitterion Chemical compound OC(=O)[C@@H](N)C1=CC=CC=C1 ZGUNAGUHMKGQNY-ZETCQYMHSA-N 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- RHGKLRLOHDJJDR-BYPYZUCNSA-N L-citrulline Chemical compound NC(=O)NCCC[C@H]([NH3+])C([O-])=O RHGKLRLOHDJJDR-BYPYZUCNSA-N 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 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
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- RHGKLRLOHDJJDR-UHFFFAOYSA-N Ndelta-carbamoyl-DL-ornithine Natural products OC(=O)C(N)CCCNC(N)=O RHGKLRLOHDJJDR-UHFFFAOYSA-N 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- AHLPHDHHMVZTML-UHFFFAOYSA-N Orn-delta-NH2 Natural products NCCCC(N)C(O)=O AHLPHDHHMVZTML-UHFFFAOYSA-N 0.000 description 1
- UTJLXEIPEHZYQJ-UHFFFAOYSA-N Ornithine Natural products OC(=O)C(C)CCCN UTJLXEIPEHZYQJ-UHFFFAOYSA-N 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 108010064851 Plant Proteins Proteins 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 108010077895 Sarcosine Proteins 0.000 description 1
- 102000013275 Somatomedins Human genes 0.000 description 1
- -1 T-BuG Chemical compound 0.000 description 1
- GKLVYJBZJHMRIY-OUBTZVSYSA-N Technetium-99 Chemical compound [99Tc] GKLVYJBZJHMRIY-OUBTZVSYSA-N 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000002730 additional effect Effects 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 230000001270 agonistic effect Effects 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 150000008064 anhydrides Chemical class 0.000 description 1
- 230000003042 antagnostic effect Effects 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000003388 anti-hormonal effect Effects 0.000 description 1
- 229940121363 anti-inflammatory agent Drugs 0.000 description 1
- 239000002260 anti-inflammatory agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 238000003149 assay kit Methods 0.000 description 1
- 235000021028 berry Nutrition 0.000 description 1
- 108010081485 beta Subunit Follicle Stimulating Hormone Proteins 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 239000003833 bile salt Substances 0.000 description 1
- 229940093761 bile salts Drugs 0.000 description 1
- 239000012472 biological sample Substances 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 229960002173 citrulline Drugs 0.000 description 1
- 235000013477 citrulline Nutrition 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 229940047120 colony stimulating factors Drugs 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 125000000151 cysteine group Chemical class N[C@@H](CS)C(=O)* 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000022811 deglycosylation Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000007933 dermal patch Substances 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 210000002249 digestive system Anatomy 0.000 description 1
- 229960003983 diphtheria toxoid Drugs 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 230000004720 fertilization Effects 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 210000003714 granulocyte Anatomy 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000003505 heat denaturation Methods 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- APFVFJFRJDLVQX-AHCXROLUSA-N indium-111 Chemical compound [111In] APFVFJFRJDLVQX-AHCXROLUSA-N 0.000 description 1
- 229940055742 indium-111 Drugs 0.000 description 1
- 208000000509 infertility Diseases 0.000 description 1
- 230000036512 infertility Effects 0.000 description 1
- 231100000535 infertility Toxicity 0.000 description 1
- 239000000893 inhibin Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 229940117681 interleukin-12 Drugs 0.000 description 1
- 229940076264 interleukin-3 Drugs 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
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000037353 metabolic pathway Effects 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 229960003104 ornithine Drugs 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 230000000149 penetrating effect Effects 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 235000021118 plant-derived protein Nutrition 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 229940043230 sarcosine Drugs 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 125000000467 secondary amino group Chemical group [H]N([*:1])[*:2] 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000003567 signal transduction assay Methods 0.000 description 1
- 229940126586 small molecule drug Drugs 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 125000001424 substituent group Chemical group 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000037317 transdermal delivery Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000013519 translation Methods 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
- 210000002700 urine Anatomy 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 230000009385 viral infection Effects 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
- C07K14/59—Follicle-stimulating hormone [FSH]; Chorionic gonadotropins, e.g.hCG [human chorionic gonadotropin]; Luteinising hormone [LH]; Thyroid-stimulating hormone [TSH]
-
- 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
-
- 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
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/10—Cells modified by introduction of foreign genetic material
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Endocrinology (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Reproductive Health (AREA)
- Wood Science & Technology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Cell Biology (AREA)
- Microbiology (AREA)
- Immunology (AREA)
- General Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Saccharide Compounds (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US28939694A | 1994-08-12 | 1994-08-12 | |
| US31059094A | 1994-09-22 | 1994-09-22 | |
| US33462994A | 1994-11-04 | 1994-11-04 | |
| US35159194A | 1994-12-07 | 1994-12-07 | |
| PCT/US1995/009664 WO1996005224A1 (fr) | 1994-08-12 | 1995-08-01 | Formes monocatenaires du quadruplet d'hormones de glycoproteine |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO961433D0 NO961433D0 (no) | 1996-04-11 |
| NO961433L NO961433L (no) | 1996-06-11 |
| NO317394B1 true NO317394B1 (no) | 2004-10-25 |
Family
ID=27501506
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO19961433A NO317394B1 (no) | 1994-08-12 | 1996-04-11 | Enkelt-kjede former av glykoprotein-hormon-kvartetten |
Country Status (14)
| Country | Link |
|---|---|
| EP (1) | EP0725795B1 (fr) |
| KR (1) | KR960704932A (fr) |
| CN (1) | CN1157408C (fr) |
| AT (1) | ATE257843T1 (fr) |
| AU (1) | AU703718B2 (fr) |
| CA (1) | CA2173750C (fr) |
| DE (1) | DE69532436T2 (fr) |
| DK (1) | DK0725795T3 (fr) |
| ES (1) | ES2210307T3 (fr) |
| FI (1) | FI120150B (fr) |
| HU (1) | HU227311B1 (fr) |
| NO (1) | NO317394B1 (fr) |
| PT (1) | PT725795E (fr) |
| WO (1) | WO1996005224A1 (fr) |
Families Citing this family (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0751782B1 (fr) * | 1994-02-18 | 2006-10-11 | Applied Research Systems ARS Holding N.V. | Utilisation d'un anticorps non-neutralisant spécifique pour la sous-unité beta de l'hormone luteinisante pour augmenter la fertilité |
| AU4964197A (en) * | 1996-11-12 | 1998-06-03 | Teikoku Hormone Mfg. Co., Ltd. | Recombinant single-stranded equine chorionic gonadotropin |
| US5883073A (en) * | 1997-04-03 | 1999-03-16 | Washington University | Single-chain double-alpha peptide |
| US6693074B1 (en) * | 1997-09-19 | 2004-02-17 | Washington University | Cystine depleted glycoprotein hormones |
| EP1017817B1 (fr) * | 1997-09-22 | 2007-03-07 | University of Maryland at Baltimore | Mutants de thyrotropine |
| US6635256B1 (en) | 1998-10-19 | 2003-10-21 | Washington University | Glycoprotein hormone compositions comprising two β subunits and methods of use thereof |
| US6103501A (en) * | 1997-11-17 | 2000-08-15 | Washington University | Single chain glycoprotein hormones comprising two β and one α subunits and recombinant production thereof |
| CA2344277A1 (fr) * | 1998-09-22 | 2000-03-30 | University Of Maryland, Baltimore | Mutants du facteur de croissance a noeud de cystine |
| JP2001333772A (ja) | 2000-04-25 | 2001-12-04 | Washington Univ | 可変性の活性を有する単鎖稔性ホルモン |
| IL154297A0 (en) * | 2000-08-11 | 2003-09-17 | Applied Res | Glycoproteins, their preparation and use |
| WO2002036626A1 (fr) * | 2000-11-02 | 2002-05-10 | Maxygen Aps | Polypeptides multimeres comportant une seule chaine |
| US6987172B2 (en) | 2001-03-05 | 2006-01-17 | Washington University In St. Louis | Multifunctional single chain glycoprotein hormones comprising three or more β subunits |
| DK1789442T3 (da) * | 2004-09-02 | 2009-11-16 | Lilly Co Eli | Muteiner af fibroblastvækstfaktor 21 |
| KR20140053991A (ko) | 2011-07-18 | 2014-05-08 | 아츠 바이올로직스 에이/에스 | 장기간 작용하는 황체 형성 호르몬 (ｌｈ) 화합물 |
| EP2968391A1 (fr) | 2013-03-13 | 2016-01-20 | Moderna Therapeutics, Inc. | Molécules polynucléotidiques à longue durée de vie |
| CN103539860B (zh) * | 2013-11-01 | 2014-12-03 | 广州优联康医药科技有限公司 | 一种长效重组人促卵泡激素融合蛋白 |
| CN103554269B (zh) * | 2013-11-01 | 2015-02-11 | 广州联康生物科技有限公司 | 重组猪促卵泡激素融合蛋白 |
| CN103539862B (zh) * | 2013-11-01 | 2015-04-01 | 广州联康生物科技有限公司 | 一种长效重组促卵泡激素及其应用 |
| CN103539861B (zh) * | 2013-11-01 | 2015-02-18 | 广州联康生物科技有限公司 | 长效重组人促卵泡激素融合蛋白 |
| BR102016006222A2 (pt) * | 2016-03-22 | 2017-09-26 | Universidade De São Paulo - Usp | Process of production and purification of recombinant hydrogen hydrogen hybrid or non-hybrid, recombinant hydrogen hydrogen hybrids or non-hybrid, vectors of expression, and uses of recombinant glicoprotetic hormones |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ATE190461T1 (de) * | 1983-11-02 | 2000-04-15 | Applied Research Systems | Produkte und methoden für die herstellung einer heterodimerer menschlicher lh mit einem met42 val55 alpha untereinheit |
| US5338835A (en) * | 1989-02-21 | 1994-08-16 | Washington University | CTP-extended form of FSH |
| DK0461200T3 (da) * | 1989-02-21 | 1997-03-10 | Univ Washington | Modificerede former af reproduktionshormoner |
| DE69131978T2 (de) * | 1990-05-08 | 2000-10-05 | Univ New Jersey Med | Glykoproteinhormon-analoga mit veränderten immunologischen merkmalen, veränderter wirksamkeit und/oder rezeptorspezifität |
-
1995
- 1995-08-01 HU HU9600948A patent/HU227311B1/hu unknown
- 1995-08-01 PT PT95928220T patent/PT725795E/pt unknown
- 1995-08-01 CA CA2173750A patent/CA2173750C/fr not_active Expired - Lifetime
- 1995-08-01 EP EP95928220A patent/EP0725795B1/fr not_active Expired - Lifetime
- 1995-08-01 CN CNB951907492A patent/CN1157408C/zh not_active Expired - Lifetime
- 1995-08-01 ES ES95928220T patent/ES2210307T3/es not_active Expired - Lifetime
- 1995-08-01 DK DK95928220T patent/DK0725795T3/da active
- 1995-08-01 DE DE69532436T patent/DE69532436T2/de not_active Expired - Lifetime
- 1995-08-01 AU AU32066/95A patent/AU703718B2/en not_active Expired
- 1995-08-01 AT AT95928220T patent/ATE257843T1/de active
- 1995-08-01 WO PCT/US1995/009664 patent/WO1996005224A1/fr active IP Right Grant
- 1995-08-01 KR KR1019960701891A patent/KR960704932A/ko active Search and Examination
-
1996
- 1996-04-11 NO NO19961433A patent/NO317394B1/no not_active IP Right Cessation
- 1996-04-11 FI FI961600A patent/FI120150B/fi not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| EP0725795A4 (fr) | 1998-05-06 |
| HUT75900A (en) | 1997-05-28 |
| NO961433D0 (no) | 1996-04-11 |
| CA2173750C (fr) | 2011-03-22 |
| NO961433L (no) | 1996-06-11 |
| WO1996005224A1 (fr) | 1996-02-22 |
| CA2173750A1 (fr) | 1996-02-22 |
| FI961600A0 (fi) | 1996-04-11 |
| CN1131952A (zh) | 1996-09-25 |
| AU703718B2 (en) | 1999-04-01 |
| PT725795E (pt) | 2004-05-31 |
| CN1157408C (zh) | 2004-07-14 |
| ATE257843T1 (de) | 2004-01-15 |
| KR960704932A (ko) | 1996-10-09 |
| ES2210307T3 (es) | 2004-07-01 |
| DE69532436T2 (de) | 2004-11-25 |
| HU227311B1 (en) | 2011-03-28 |
| EP0725795A1 (fr) | 1996-08-14 |
| AU3206695A (en) | 1996-03-07 |
| FI961600A (fi) | 1996-04-11 |
| DK0725795T3 (da) | 2004-05-17 |
| EP0725795B1 (fr) | 2004-01-14 |
| DE69532436D1 (de) | 2004-02-19 |
| FI120150B (fi) | 2009-07-15 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5705478A (en) | Covalently linked β subunits of the glycoprotein hormones as antagonists | |
| US6238890B1 (en) | Single chain forms of the glycoprotein hormone quartet | |
| US5958737A (en) | Single-chain β subunit dimers of the glycoprotein hormones and recombinant materials related thereto | |
| AU754296B2 (en) | Single-chain bifunctional glycoprotein hormones | |
| NO317394B1 (no) | Enkelt-kjede former av glykoprotein-hormon-kvartetten | |
| US6028177A (en) | Methods of detecting single-chain forms of the glycoprotein hormone quartet | |
| US20020160944A1 (en) | Multifunctional single chain glycoprotein hormones | |
| KR20020006720A (ko) | 이황화결합으로 연결된 당단백질 호르몬 유사체, 이의제조방법 및 이의 용도 | |
| US5883073A (en) | Single-chain double-alpha peptide | |
| US6635256B1 (en) | Glycoprotein hormone compositions comprising two β subunits and methods of use thereof | |
| JP2009050278A (ja) | 糖タンパク質ホルモンカルテットの一本鎖形態 | |
| US6693074B1 (en) | Cystine depleted glycoprotein hormones | |
| EP1276765A2 (fr) | Hormones de fertilite a une seule chaine avec activite lh variable | |
| MXPA01003947A (en) | Multiple domain glycoprotein hormones and methods of using | |
| MXPA00004761A (en) | Single-chain bifunctional glycoprotein hormones |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MK1K | Patent expired |