PT94241A - Processo para a preparacao de factor calcificacao ossea e de composicoes farmaceuticas que os contem - Google Patents
Processo para a preparacao de factor calcificacao ossea e de composicoes farmaceuticas que os contem Download PDFInfo
- Publication number
- PT94241A PT94241A PT94241A PT9424190A PT94241A PT 94241 A PT94241 A PT 94241A PT 94241 A PT94241 A PT 94241A PT 9424190 A PT9424190 A PT 9424190A PT 94241 A PT94241 A PT 94241A
- Authority
- PT
- Portugal
- Prior art keywords
- tyr
- gly
- tac
- glu
- tgg
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims 38
- 230000002308 calcification Effects 0.000 title claims 5
- 239000008194 pharmaceutical composition Substances 0.000 title claims 3
- 241000283690 Bos taurus Species 0.000 claims 26
- 230000018678 bone mineralization Effects 0.000 claims 10
- 210000004027 cell Anatomy 0.000 claims 10
- 108090000765 processed proteins & peptides Proteins 0.000 claims 10
- COYHRQWNJDJCNA-NUJDXYNKSA-N Thr-Thr-Thr Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O COYHRQWNJDJCNA-NUJDXYNKSA-N 0.000 claims 8
- 239000012634 fragment Substances 0.000 claims 8
- 108020004414 DNA Proteins 0.000 claims 7
- 108010076504 Protein Sorting Signals Proteins 0.000 claims 6
- 229920001184 polypeptide Polymers 0.000 claims 6
- 102000004196 processed proteins & peptides Human genes 0.000 claims 6
- 150000001413 amino acids Chemical group 0.000 claims 5
- YJHKTAMKPGFJCT-NRPADANISA-N Ala-Val-Glu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(O)=O YJHKTAMKPGFJCT-NRPADANISA-N 0.000 claims 4
- ZWMYUDZLXAQHCK-CIUDSAMLSA-N Glu-Met-Asp Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(O)=O ZWMYUDZLXAQHCK-CIUDSAMLSA-N 0.000 claims 4
- PMGDADKJMCOXHX-UHFFFAOYSA-N L-Arginyl-L-glutamin-acetat Natural products NC(=N)NCCCC(N)C(=O)NC(CCC(N)=O)C(O)=O PMGDADKJMCOXHX-UHFFFAOYSA-N 0.000 claims 4
- YKNBJXOJTURHCU-DCAQKATOSA-N Leu-Asp-Arg Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCN=C(N)N YKNBJXOJTURHCU-DCAQKATOSA-N 0.000 claims 4
- JUXONJROIXKHEV-GUBZILKMSA-N Met-Cys-Arg Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CS)C(=O)N[C@H](C(O)=O)CCCNC(N)=N JUXONJROIXKHEV-GUBZILKMSA-N 0.000 claims 4
- AJHCSUXXECOXOY-UHFFFAOYSA-N N-glycyl-L-tryptophan Natural products C1=CC=C2C(CC(NC(=O)CN)C(O)=O)=CNC2=C1 AJHCSUXXECOXOY-UHFFFAOYSA-N 0.000 claims 4
- 108091028043 Nucleic acid sequence Proteins 0.000 claims 4
- CVAUVSOFHJKCHN-BZSNNMDCSA-N Phe-Tyr-Cys Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CS)C(O)=O)C1=CC=CC=C1 CVAUVSOFHJKCHN-BZSNNMDCSA-N 0.000 claims 4
- KZTLJLFVOIMRAQ-IHPCNDPISA-N Trp-Asn-Tyr Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O KZTLJLFVOIMRAQ-IHPCNDPISA-N 0.000 claims 4
- 108010047495 alanylglycine Proteins 0.000 claims 4
- 108010013835 arginine glutamate Proteins 0.000 claims 4
- 108010008355 arginyl-glutamine Proteins 0.000 claims 4
- 108010068265 aspartyltyrosine Proteins 0.000 claims 4
- 239000013611 chromosomal DNA Substances 0.000 claims 4
- 108010004073 cysteinylcysteine Proteins 0.000 claims 4
- 108010084389 glycyltryptophan Proteins 0.000 claims 4
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims 4
- XVLLUZMFSAYKJV-GUBZILKMSA-N Arg-Asp-Arg Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O XVLLUZMFSAYKJV-GUBZILKMSA-N 0.000 claims 3
- FANQWNCPNFEPGZ-WHFBIAKZSA-N Asp-Asp-Gly Chemical group [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(O)=O FANQWNCPNFEPGZ-WHFBIAKZSA-N 0.000 claims 3
- XXDLUZLKHOVPNW-IHRRRGAJSA-N Cys-Arg-Tyr Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)O)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CS)N)O XXDLUZLKHOVPNW-IHRRRGAJSA-N 0.000 claims 3
- BETSEXMYBWCDAE-SZMVWBNQSA-N Gln-Trp-Lys Chemical compound C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)N[C@@H](CCCCN)C(=O)O)NC(=O)[C@H](CCC(=O)N)N BETSEXMYBWCDAE-SZMVWBNQSA-N 0.000 claims 3
- SGVGIVDZLSHSEN-RYUDHWBXSA-N Gln-Tyr-Gly Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)NCC(O)=O SGVGIVDZLSHSEN-RYUDHWBXSA-N 0.000 claims 3
- ZNOHKCPYDAYYDA-BPUTZDHNSA-N Glu-Trp-Gln Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CCC(N)=O)C(O)=O ZNOHKCPYDAYYDA-BPUTZDHNSA-N 0.000 claims 3
- CGWHAXBNGYQBBK-JBACZVJFSA-N Glu-Trp-Tyr Chemical compound C([C@H](NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CCC(O)=O)N)C(O)=O)C1=CC=C(O)C=C1 CGWHAXBNGYQBBK-JBACZVJFSA-N 0.000 claims 3
- YYXJFBMCOUSYSF-RYUDHWBXSA-N Gly-Phe-Gln Chemical compound [H]NCC(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCC(N)=O)C(O)=O YYXJFBMCOUSYSF-RYUDHWBXSA-N 0.000 claims 3
- PZUZIHRPOVVHOT-KBPBESRZSA-N His-Tyr-Gly Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)NCC(O)=O)C1=CN=CN1 PZUZIHRPOVVHOT-KBPBESRZSA-N 0.000 claims 3
- KGCLIYGPQXUNLO-IUCAKERBSA-N Leu-Gly-Glu Chemical compound CC(C)C[C@H](N)C(=O)NCC(=O)N[C@H](C(O)=O)CCC(O)=O KGCLIYGPQXUNLO-IUCAKERBSA-N 0.000 claims 3
- MKBVYCVTDBHWSZ-DCAQKATOSA-N Leu-Val-Ala Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C)C(O)=O MKBVYCVTDBHWSZ-DCAQKATOSA-N 0.000 claims 3
- AIOWVDNPESPXRB-YTWAJWBKSA-N Pro-Thr-Pro Chemical compound C[C@H]([C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@@H]2CCCN2)O AIOWVDNPESPXRB-YTWAJWBKSA-N 0.000 claims 3
- LWMQRHDTXHQQOV-MXAVVETBSA-N Ser-Ile-Phe Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O LWMQRHDTXHQQOV-MXAVVETBSA-N 0.000 claims 3
- VBMOVTMNHWPZJR-SUSMZKCASA-N Thr-Thr-Glu Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(O)=O)C(O)=O VBMOVTMNHWPZJR-SUSMZKCASA-N 0.000 claims 3
- HGEHWFGAKHSIDY-SRVKXCTJSA-N Tyr-Asp-Cys Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CS)C(=O)O)N)O HGEHWFGAKHSIDY-SRVKXCTJSA-N 0.000 claims 3
- QRZVUAAKNRHEOP-GUBZILKMSA-N Val-Ala-Val Chemical compound [H]N[C@@H](C(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(O)=O QRZVUAAKNRHEOP-GUBZILKMSA-N 0.000 claims 3
- 239000003795 chemical substances by application Substances 0.000 claims 3
- 108010020688 glycylhistidine Proteins 0.000 claims 3
- 108010038320 lysylphenylalanine Proteins 0.000 claims 3
- 239000000203 mixture Substances 0.000 claims 3
- 108010079317 prolyl-tyrosine Proteins 0.000 claims 3
- 108010079202 tyrosyl-alanyl-cysteine Proteins 0.000 claims 3
- XYKDZXKKYOOTGC-FXQIFTODSA-N Ala-Cys-Met Chemical compound C[C@@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CCSC)C(=O)O)N XYKDZXKKYOOTGC-FXQIFTODSA-N 0.000 claims 2
- CWEAKSWWKHGTRJ-BQBZGAKWSA-N Ala-Gly-Met Chemical compound [H]N[C@@H](C)C(=O)NCC(=O)N[C@@H](CCSC)C(O)=O CWEAKSWWKHGTRJ-BQBZGAKWSA-N 0.000 claims 2
- KUFVXLQLDHJVOG-SHGPDSBTSA-N Ala-Thr-Thr Chemical compound C[C@H]([C@@H](C(=O)N[C@@H]([C@@H](C)O)C(=O)O)NC(=O)[C@H](C)N)O KUFVXLQLDHJVOG-SHGPDSBTSA-N 0.000 claims 2
- LFWOQHSQNCKXRU-UFYCRDLUSA-N Arg-Tyr-Phe Chemical compound C([C@H](NC(=O)[C@H](CCCN=C(N)N)N)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=C(O)C=C1 LFWOQHSQNCKXRU-UFYCRDLUSA-N 0.000 claims 2
- PCKRJVZAQZWNKM-WHFBIAKZSA-N Asn-Asn-Gly Chemical compound NC(=O)C[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(O)=O PCKRJVZAQZWNKM-WHFBIAKZSA-N 0.000 claims 2
- SKQTXVZTCGSRJS-SRVKXCTJSA-N Asn-Tyr-Asp Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)O)NC(=O)[C@H](CC(=O)N)N)O SKQTXVZTCGSRJS-SRVKXCTJSA-N 0.000 claims 2
- PSZNHSNIGMJYOZ-WDSKDSINSA-N Asp-Arg Chemical compound OC(=O)C[C@H](N)C(=O)N[C@H](C(O)=O)CCCN=C(N)N PSZNHSNIGMJYOZ-WDSKDSINSA-N 0.000 claims 2
- ALMIMUZAWTUNIO-BZSNNMDCSA-N Asp-Tyr-Tyr Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O ALMIMUZAWTUNIO-BZSNNMDCSA-N 0.000 claims 2
- 101100290999 Bos taurus MET gene Proteins 0.000 claims 2
- JUNZLDGUJZIUCO-IHRRRGAJSA-N Cys-Pro-Tyr Chemical compound C1C[C@H](N(C1)C(=O)[C@H](CS)N)C(=O)N[C@@H](CC2=CC=C(C=C2)O)C(=O)O JUNZLDGUJZIUCO-IHRRRGAJSA-N 0.000 claims 2
- SDSMVVSHLAAOJL-UKJIMTQDSA-N Gln-Val-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CCC(=O)N)N SDSMVVSHLAAOJL-UKJIMTQDSA-N 0.000 claims 2
- PMSMKNYRZCKVMC-DRZSPHRISA-N Glu-Phe-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CC1=CC=CC=C1)NC(=O)[C@H](CCC(=O)O)N PMSMKNYRZCKVMC-DRZSPHRISA-N 0.000 claims 2
- SJLKKOZFHSJJAW-YUMQZZPRSA-N Gly-Met-Glu Chemical compound CSCC[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC(=O)CN SJLKKOZFHSJJAW-YUMQZZPRSA-N 0.000 claims 2
- 102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 claims 2
- 101000773083 Homo sapiens 5,6-dihydroxyindole-2-carboxylic acid oxidase Proteins 0.000 claims 2
- 101000664418 Homo sapiens Secreted Ly-6/uPAR-related protein 1 Proteins 0.000 claims 2
- QLRMMMQNCWBNPQ-QXEWZRGKSA-N Ile-Arg-Gly Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)NCC(=O)O)N QLRMMMQNCWBNPQ-QXEWZRGKSA-N 0.000 claims 2
- YKRIXHPEIZUDDY-GMOBBJLQSA-N Ile-Asn-Arg Chemical compound CC[C@H](C)[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(O)=O)CCCN=C(N)N YKRIXHPEIZUDDY-GMOBBJLQSA-N 0.000 claims 2
- IGUOAYLTQJLPPD-DCAQKATOSA-N Leu-Asn-Arg Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(O)=O)CCCN=C(N)N IGUOAYLTQJLPPD-DCAQKATOSA-N 0.000 claims 2
- UQRZFMQQXXJTTF-AVGNSLFASA-N Lys-Lys-Glu Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O UQRZFMQQXXJTTF-AVGNSLFASA-N 0.000 claims 2
- FWAHLGXNBLWIKB-NAKRPEOUSA-N Met-Ile-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H](N)CCSC FWAHLGXNBLWIKB-NAKRPEOUSA-N 0.000 claims 2
- KYXDADPHSNFWQX-VEVYYDQMSA-N Met-Thr-Asp Chemical compound CSCC[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@H](C(O)=O)CC(O)=O KYXDADPHSNFWQX-VEVYYDQMSA-N 0.000 claims 2
- 108010079364 N-glycylalanine Proteins 0.000 claims 2
- IURWWZYKYPEANQ-HJGDQZAQSA-N Pro-Thr-Glu Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(O)=O)C(O)=O IURWWZYKYPEANQ-HJGDQZAQSA-N 0.000 claims 2
- GRRAECZXRONTEE-UBHSHLNASA-N Ser-Cys-Trp Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(O)=O GRRAECZXRONTEE-UBHSHLNASA-N 0.000 claims 2
- NNFMANHDYSVNIO-DCAQKATOSA-N Ser-Lys-Arg Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O NNFMANHDYSVNIO-DCAQKATOSA-N 0.000 claims 2
- CZWIHKFGHICAJX-BPUTZDHNSA-N Trp-Glu-Glu Chemical compound C1=CC=C2C(C[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O)=CNC2=C1 CZWIHKFGHICAJX-BPUTZDHNSA-N 0.000 claims 2
- XKTWZYNTLXITCY-QRTARXTBSA-N Trp-Val-Asn Chemical compound C1=CC=C2C(C[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(N)=O)C(O)=O)=CNC2=C1 XKTWZYNTLXITCY-QRTARXTBSA-N 0.000 claims 2
- NSTPFWRAIDTNGH-BZSNNMDCSA-N Tyr-Asn-Tyr Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O NSTPFWRAIDTNGH-BZSNNMDCSA-N 0.000 claims 2
- LRHBBGDMBLFYGL-FHWLQOOXSA-N Tyr-Phe-Glu Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCC(O)=O)C(O)=O)C1=CC=C(O)C=C1 LRHBBGDMBLFYGL-FHWLQOOXSA-N 0.000 claims 2
- SZEIFUXUTBBQFQ-STQMWFEESA-N Tyr-Pro-Gly Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N1CCC[C@H]1C(=O)NCC(O)=O SZEIFUXUTBBQFQ-STQMWFEESA-N 0.000 claims 2
- 241000251539 Vertebrata <Metazoa> Species 0.000 claims 2
- 210000000988 bone and bone Anatomy 0.000 claims 2
- 230000000295 complement effect Effects 0.000 claims 2
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 claims 2
- VPZXBVLAVMBEQI-UHFFFAOYSA-N glycyl-DL-alpha-alanine Natural products OC(=O)C(C)NC(=O)CN VPZXBVLAVMBEQI-UHFFFAOYSA-N 0.000 claims 2
- 108010050848 glycylleucine Proteins 0.000 claims 2
- 102000049578 human SLURP1 Human genes 0.000 claims 2
- 108010078274 isoleucylvaline Proteins 0.000 claims 2
- 108010056582 methionylglutamic acid Proteins 0.000 claims 2
- 239000002773 nucleotide Substances 0.000 claims 2
- 125000003729 nucleotide group Chemical group 0.000 claims 2
- 108010012581 phenylalanylglutamate Proteins 0.000 claims 2
- 108010051242 phenylalanylserine Proteins 0.000 claims 2
- 239000000126 substance Substances 0.000 claims 2
- 108010033670 threonyl-aspartyl-tyrosine Proteins 0.000 claims 2
- ZIBWKCRKNFYTPT-ZKWXMUAHSA-N Ala-Asn-Val Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C(C)C)C(O)=O ZIBWKCRKNFYTPT-ZKWXMUAHSA-N 0.000 claims 1
- PWYFCPCBOYMOGB-LKTVYLICSA-N Ala-Gln-Trp Chemical compound C[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC1=CNC2=CC=CC=C21)C(=O)O)N PWYFCPCBOYMOGB-LKTVYLICSA-N 0.000 claims 1
- QHASENCZLDHBGX-ONGXEEELSA-N Ala-Gly-Phe Chemical compound C[C@H](N)C(=O)NCC(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 QHASENCZLDHBGX-ONGXEEELSA-N 0.000 claims 1
- 102100034044 All-trans-retinol dehydrogenase [NAD(+)] ADH1B Human genes 0.000 claims 1
- 101710193111 All-trans-retinol dehydrogenase [NAD(+)] ADH4 Proteins 0.000 claims 1
- 241000224489 Amoeba Species 0.000 claims 1
- SIFXMYAHXJGAFC-WDSKDSINSA-N Arg-Asp Chemical compound NC(=N)NCCC[C@H](N)C(=O)N[C@@H](CC(O)=O)C(O)=O SIFXMYAHXJGAFC-WDSKDSINSA-N 0.000 claims 1
- AQPVUEJJARLJHB-BQBZGAKWSA-N Arg-Gly-Ala Chemical compound OC(=O)[C@H](C)NC(=O)CNC(=O)[C@@H](N)CCCN=C(N)N AQPVUEJJARLJHB-BQBZGAKWSA-N 0.000 claims 1
- UVTGNSWSRSCPLP-UHFFFAOYSA-N Arg-Tyr Natural products NC(CCNC(=N)N)C(=O)NC(Cc1ccc(O)cc1)C(=O)O UVTGNSWSRSCPLP-UHFFFAOYSA-N 0.000 claims 1
- VDCIPFYVCICPEC-FXQIFTODSA-N Asn-Arg-Ala Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(O)=O VDCIPFYVCICPEC-FXQIFTODSA-N 0.000 claims 1
- ZMUQQMGITUJQTI-CIUDSAMLSA-N Asn-Leu-Asn Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(O)=O ZMUQQMGITUJQTI-CIUDSAMLSA-N 0.000 claims 1
- ZYPWIUFLYMQZBS-SRVKXCTJSA-N Asn-Lys-Lys Chemical compound C(CCN)C[C@@H](C(=O)N[C@@H](CCCCN)C(=O)O)NC(=O)[C@H](CC(=O)N)N ZYPWIUFLYMQZBS-SRVKXCTJSA-N 0.000 claims 1
- SOYOSFXLXYZNRG-CIUDSAMLSA-N Asp-Arg-Gln Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(O)=O SOYOSFXLXYZNRG-CIUDSAMLSA-N 0.000 claims 1
- AWPWHMVCSISSQK-QWRGUYRKSA-N Asp-Tyr-Gly Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)NCC(O)=O AWPWHMVCSISSQK-QWRGUYRKSA-N 0.000 claims 1
- 101100045551 Bos taurus TBPL1 gene Proteins 0.000 claims 1
- QLCPDGRAEJSYQM-LPEHRKFASA-N Cys-Arg-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CS)N)C(=O)O QLCPDGRAEJSYQM-LPEHRKFASA-N 0.000 claims 1
- UYYZZJXUVIZTMH-AVGNSLFASA-N Cys-Glu-Phe Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O UYYZZJXUVIZTMH-AVGNSLFASA-N 0.000 claims 1
- TXCCRYAZQBUCOV-CIUDSAMLSA-N Cys-Pro-Gln Chemical compound [H]N[C@@H](CS)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(O)=O TXCCRYAZQBUCOV-CIUDSAMLSA-N 0.000 claims 1
- MSWBLPLBSLQVME-XIRDDKMYSA-N Cys-Trp-Leu Chemical compound C1=CC=C2C(C[C@@H](C(=O)N[C@@H](CC(C)C)C(O)=O)NC(=O)[C@@H](N)CS)=CNC2=C1 MSWBLPLBSLQVME-XIRDDKMYSA-N 0.000 claims 1
- LOJYQMFIIJVETK-WDSKDSINSA-N Gln-Gln Chemical compound NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(O)=O LOJYQMFIIJVETK-WDSKDSINSA-N 0.000 claims 1
- FGYPOQPQTUNESW-IUCAKERBSA-N Gln-Gly-Leu Chemical compound CC(C)C[C@@H](C(=O)O)NC(=O)CNC(=O)[C@H](CCC(=O)N)N FGYPOQPQTUNESW-IUCAKERBSA-N 0.000 claims 1
- NYCVMJGIJYQWDO-CIUDSAMLSA-N Gln-Ser-Arg Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O NYCVMJGIJYQWDO-CIUDSAMLSA-N 0.000 claims 1
- XIYWAJQIWLXXAF-XKBZYTNZSA-N Gln-Thr-Cys Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CS)C(=O)O)NC(=O)[C@H](CCC(=O)N)N)O XIYWAJQIWLXXAF-XKBZYTNZSA-N 0.000 claims 1
- BJVBMSTUUWGZKX-JYJNAYRXSA-N Gln-Tyr-His Chemical compound N[C@@H](CCC(N)=O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1cnc[nH]1)C(O)=O BJVBMSTUUWGZKX-JYJNAYRXSA-N 0.000 claims 1
- SOEXCCGNHQBFPV-DLOVCJGASA-N Gln-Val-Val Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(O)=O SOEXCCGNHQBFPV-DLOVCJGASA-N 0.000 claims 1
- HHSKZJZWQFPSKN-AVGNSLFASA-N Glu-Tyr-Asp Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(O)=O)C(O)=O HHSKZJZWQFPSKN-AVGNSLFASA-N 0.000 claims 1
- KXRORHJIRAOQPG-SOUVJXGZSA-N Glu-Tyr-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CC2=CC=C(C=C2)O)NC(=O)[C@H](CCC(=O)O)N)C(=O)O KXRORHJIRAOQPG-SOUVJXGZSA-N 0.000 claims 1
- BEQGFMIBZFNROK-JGVFFNPUSA-N Gly-Glu-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CCC(=O)O)NC(=O)CN)C(=O)O BEQGFMIBZFNROK-JGVFFNPUSA-N 0.000 claims 1
- YNIMVVJTPWCUJH-KBPBESRZSA-N Gly-His-Tyr Chemical compound [H]NCC(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O YNIMVVJTPWCUJH-KBPBESRZSA-N 0.000 claims 1
- MIIVFRCYJABHTQ-ONGXEEELSA-N Gly-Leu-Val Chemical compound [H]NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(O)=O MIIVFRCYJABHTQ-ONGXEEELSA-N 0.000 claims 1
- OHUKZZYSJBKFRR-WHFBIAKZSA-N Gly-Ser-Asp Chemical compound [H]NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(O)=O OHUKZZYSJBKFRR-WHFBIAKZSA-N 0.000 claims 1
- LYZYGGWCBLBDMC-QWHCGFSZSA-N Gly-Tyr-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CC2=CC=C(C=C2)O)NC(=O)CN)C(=O)O LYZYGGWCBLBDMC-QWHCGFSZSA-N 0.000 claims 1
- DNAZKGFYFRGZIH-QWRGUYRKSA-N Gly-Tyr-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)CN)CC1=CC=C(O)C=C1 DNAZKGFYFRGZIH-QWRGUYRKSA-N 0.000 claims 1
- LBHOVGUGOBINDL-KKUMJFAQSA-N His-Asp-Tyr Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC2=CN=CN2)N)O LBHOVGUGOBINDL-KKUMJFAQSA-N 0.000 claims 1
- JFFAPRNXXLRINI-NHCYSSNCSA-N His-Asp-Val Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(O)=O JFFAPRNXXLRINI-NHCYSSNCSA-N 0.000 claims 1
- FMRKUXFLLPKVPG-JYJNAYRXSA-N His-Gln-Tyr Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)O)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H](CC2=CN=CN2)N)O FMRKUXFLLPKVPG-JYJNAYRXSA-N 0.000 claims 1
- LEDRIAHEWDJRMF-CFMVVWHZSA-N Ile-Asn-Tyr Chemical compound CC[C@H](C)[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 LEDRIAHEWDJRMF-CFMVVWHZSA-N 0.000 claims 1
- WLRJHVNFGAOYPS-HJPIBITLSA-N Ile-Ser-Tyr Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)O)N WLRJHVNFGAOYPS-HJPIBITLSA-N 0.000 claims 1
- TYYLDKGBCJGJGW-UHFFFAOYSA-N L-tryptophan-L-tyrosine Natural products C=1NC2=CC=CC=C2C=1CC(N)C(=O)NC(C(O)=O)CC1=CC=C(O)C=C1 TYYLDKGBCJGJGW-UHFFFAOYSA-N 0.000 claims 1
- 241000880493 Leptailurus serval Species 0.000 claims 1
- SQUFDMCWMFOEBA-KKUMJFAQSA-N Leu-Ser-Tyr Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 SQUFDMCWMFOEBA-KKUMJFAQSA-N 0.000 claims 1
- NPBGTPKLVJEOBE-IUCAKERBSA-N Lys-Arg Chemical compound NCCCC[C@H](N)C(=O)N[C@H](C(O)=O)CCCNC(N)=N NPBGTPKLVJEOBE-IUCAKERBSA-N 0.000 claims 1
- ZTPWXNOOKAXPPE-DCAQKATOSA-N Lys-Arg-Cys Chemical compound C(CCN)C[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CS)C(=O)O)N ZTPWXNOOKAXPPE-DCAQKATOSA-N 0.000 claims 1
- LMGNWHDWJDIOPK-DKIMLUQUSA-N Lys-Phe-Ile Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O LMGNWHDWJDIOPK-DKIMLUQUSA-N 0.000 claims 1
- 241000124008 Mammalia Species 0.000 claims 1
- DSWOTZCVCBEPOU-IUCAKERBSA-N Met-Arg-Gly Chemical compound CSCC[C@H](N)C(=O)N[C@H](C(=O)NCC(O)=O)CCCNC(N)=N DSWOTZCVCBEPOU-IUCAKERBSA-N 0.000 claims 1
- GMMLGMFBYCFCCX-KZVJFYERSA-N Met-Thr-Ala Chemical compound CSCC[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C)C(O)=O GMMLGMFBYCFCCX-KZVJFYERSA-N 0.000 claims 1
- FXBKQTOGURNXSL-HJGDQZAQSA-N Met-Thr-Glu Chemical compound CSCC[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@H](C(O)=O)CCC(O)=O FXBKQTOGURNXSL-HJGDQZAQSA-N 0.000 claims 1
- ZPPVJIJMIKTERM-YUMQZZPRSA-N Pro-Gln-Gly Chemical compound OC(=O)CNC(=O)[C@H](CCC(=O)N)NC(=O)[C@@H]1CCCN1 ZPPVJIJMIKTERM-YUMQZZPRSA-N 0.000 claims 1
- VWXGFAIZUQBBBG-UWVGGRQHSA-N Pro-His-Gly Chemical compound C([C@@H](C(=O)NCC(=O)[O-])NC(=O)[C@H]1[NH2+]CCC1)C1=CN=CN1 VWXGFAIZUQBBBG-UWVGGRQHSA-N 0.000 claims 1
- RCYUBVHMVUHEBM-RCWTZXSCSA-N Pro-Pro-Thr Chemical compound [H]N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)O)C(O)=O RCYUBVHMVUHEBM-RCWTZXSCSA-N 0.000 claims 1
- OIDKVWTWGDWMHY-RYUDHWBXSA-N Pro-Tyr Chemical compound C([C@@H](C(=O)O)NC(=O)[C@H]1NCCC1)C1=CC=C(O)C=C1 OIDKVWTWGDWMHY-RYUDHWBXSA-N 0.000 claims 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims 1
- HQTKVSCNCDLXSX-BQBZGAKWSA-N Ser-Arg-Gly Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(O)=O HQTKVSCNCDLXSX-BQBZGAKWSA-N 0.000 claims 1
- OOKCGAYXSNJBGQ-ZLUOBGJFSA-N Ser-Asn-Asn Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O OOKCGAYXSNJBGQ-ZLUOBGJFSA-N 0.000 claims 1
- LQESNKGTTNHZPZ-GHCJXIJMSA-N Ser-Ile-Asn Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(O)=O LQESNKGTTNHZPZ-GHCJXIJMSA-N 0.000 claims 1
- CRJZZXMAADSBBQ-SRVKXCTJSA-N Ser-Lys-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CO CRJZZXMAADSBBQ-SRVKXCTJSA-N 0.000 claims 1
- VEVYMLNYMULSMS-AVGNSLFASA-N Ser-Tyr-Gln Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CCC(N)=O)C(O)=O VEVYMLNYMULSMS-AVGNSLFASA-N 0.000 claims 1
- LLSLRQOEAFCZLW-NRPADANISA-N Ser-Val-Gln Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O LLSLRQOEAFCZLW-NRPADANISA-N 0.000 claims 1
- CUTPSEKWUPZFLV-WISUUJSJSA-N Thr-Cys Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](CS)C(O)=O CUTPSEKWUPZFLV-WISUUJSJSA-N 0.000 claims 1
- MMTOHPRBJKEZHT-BWBBJGPYSA-N Thr-Cys-Ser Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](CO)C(O)=O MMTOHPRBJKEZHT-BWBBJGPYSA-N 0.000 claims 1
- VOHWDZNIESHTFW-XKBZYTNZSA-N Thr-Glu-Cys Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CS)C(=O)O)N)O VOHWDZNIESHTFW-XKBZYTNZSA-N 0.000 claims 1
- HOJPPPKZWFRTHJ-PJODQICGSA-N Trp-Arg-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC1=CNC2=CC=CC=C21)N HOJPPPKZWFRTHJ-PJODQICGSA-N 0.000 claims 1
- YEGMNOHLZNGOCG-UBHSHLNASA-N Trp-Asn-Asn Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O YEGMNOHLZNGOCG-UBHSHLNASA-N 0.000 claims 1
- WPSYJHFHZYJXMW-JSGCOSHPSA-N Trp-Gln-Gly Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(O)=O WPSYJHFHZYJXMW-JSGCOSHPSA-N 0.000 claims 1
- WCTYCXZYBNKEIV-SXNHZJKMSA-N Trp-Glu-Ile Chemical compound C1=CC=C2C(C[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O)=CNC2=C1 WCTYCXZYBNKEIV-SXNHZJKMSA-N 0.000 claims 1
- UJRIVCPPPMYCNA-HOCLYGCPSA-N Trp-Leu-Gly Chemical compound CC(C)C[C@@H](C(=O)NCC(=O)O)NC(=O)[C@H](CC1=CNC2=CC=CC=C21)N UJRIVCPPPMYCNA-HOCLYGCPSA-N 0.000 claims 1
- CWQZAUYFWRLITN-AVGNSLFASA-N Tyr-Gln-Cys Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CS)C(=O)O)N)O CWQZAUYFWRLITN-AVGNSLFASA-N 0.000 claims 1
- AKLNEFNQWLHIGY-QWRGUYRKSA-N Tyr-Gly-Asp Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)NCC(=O)N[C@@H](CC(=O)O)C(=O)O)N)O AKLNEFNQWLHIGY-QWRGUYRKSA-N 0.000 claims 1
- NMKJPMCEKQHRPD-IRXDYDNUSA-N Tyr-Gly-Tyr Chemical compound C([C@H](N)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)C1=CC=C(O)C=C1 NMKJPMCEKQHRPD-IRXDYDNUSA-N 0.000 claims 1
- KWKJGBHDYJOVCR-SRVKXCTJSA-N Tyr-Ser-Cys Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CS)C(=O)O)N)O KWKJGBHDYJOVCR-SRVKXCTJSA-N 0.000 claims 1
- MDXLPNRXCFOBTL-BZSNNMDCSA-N Tyr-Ser-Tyr Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O MDXLPNRXCFOBTL-BZSNNMDCSA-N 0.000 claims 1
- BUPRFDPUIJNOLS-UFYCRDLUSA-N Tyr-Tyr-Met Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CCSC)C(O)=O BUPRFDPUIJNOLS-UFYCRDLUSA-N 0.000 claims 1
- 108010070783 alanyltyrosine Proteins 0.000 claims 1
- 230000015572 biosynthetic process Effects 0.000 claims 1
- 230000037396 body weight Effects 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 108010060199 cysteinylproline Proteins 0.000 claims 1
- 238000012217 deletion Methods 0.000 claims 1
- 230000037430 deletion Effects 0.000 claims 1
- 239000003937 drug carrier Substances 0.000 claims 1
- 210000003527 eukaryotic cell Anatomy 0.000 claims 1
- XBGGUPMXALFZOT-UHFFFAOYSA-N glycyl-L-tyrosine hemihydrate Natural products NCC(=O)NC(C(O)=O)CC1=CC=C(O)C=C1 XBGGUPMXALFZOT-UHFFFAOYSA-N 0.000 claims 1
- 108010027668 glycyl-alanyl-valine Proteins 0.000 claims 1
- 108010087823 glycyltyrosine Proteins 0.000 claims 1
- 102000057421 human MET Human genes 0.000 claims 1
- 230000000977 initiatory effect Effects 0.000 claims 1
- 108010066733 mRNA (guanine(N7))-methyltransferase Proteins 0.000 claims 1
- 102000043253 matrix Gla protein Human genes 0.000 claims 1
- 108010057546 matrix Gla protein Proteins 0.000 claims 1
- 230000002138 osteoinductive effect Effects 0.000 claims 1
- 238000012207 quantitative assay Methods 0.000 claims 1
- 108010080629 tryptophan-leucine Proteins 0.000 claims 1
- 108010044292 tryptophyltyrosine Proteins 0.000 claims 1
- 108010020532 tyrosyl-proline Proteins 0.000 claims 1
- 108010021199 valyl-valyl-valine Proteins 0.000 claims 1
- 108010073969 valyllysine Proteins 0.000 claims 1
- 210000002268 wool Anatomy 0.000 claims 1
Classifications
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/80—Vectors or expression systems specially adapted for eukaryotic hosts for fungi
- C12N15/81—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/12—Drugs for disorders of the metabolism for electrolyte homeostasis
- A61P3/14—Drugs for disorders of the metabolism for electrolyte homeostasis for calcium homeostasis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- 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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- 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
- C07K14/475—Growth factors; Growth regulators
- C07K14/51—Bone morphogenetic factor; Osteogenins; Osteogenic factor; Bone-inducing factor
-
- 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
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
-
- 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
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
- C12N15/625—DNA sequences coding for fusion proteins containing a sequence coding for a signal sequence
-
- 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
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/036—Fusion polypeptide containing a localisation/targetting motif targeting to the medium outside of the cell, e.g. type III secretion
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Wood Science & Technology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Mycology (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Obesity (AREA)
- Diabetes (AREA)
- Hematology (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Rheumatology (AREA)
- Endocrinology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Claims (2)
- 32 'Th REIVINDICAÇÕES: lã. - processo para a preparação de factor de calcificação óssea, caracterizado pelo facto de cpmpreender as operações que consistem em se construir um vector que inclui c l seguinte sequên cia de ADN humano. CAG TAT GGC GAT TAT GGA TAC CCA TAC humano CAG CAG TAT CAT GAC TAC AGC GAT GAT GGG TGG GTG AAT TTG AAC CGG CAA GGC TTC AGC TAC CAG TGT CCC CAG GGG CAG GTG ATA GTG GCC GTG humano AGG AGC ATC TTC AGC AAG AAG GAA GGT TCT GAC AGA CAA TGG AAC TAC GCC TGC ATG CCC ACG CCA CAG AGC CTC GGG GAA CCC ACG GAG TGC TGG humano TGG GAG GAG ATC AAC AGG GTC GGC ATG GCT GGC ATG GAA TGG TAC CAG ACG TGC TCC AAC AAT GGG CTG GTG GCA GGA TTC CAG AGC CGC TAC TTC GAG TCA GTG humano CTG GAT CGG GAG TGG CAG TTT TAC TGT TGT CGC TAC AGC AAG AGA TGC CCA TAT TCC TGC TGG CTA ACA ACA GAA TAT CCA GGT CAC TAT GGT GA humano GAG ATG GAC ATG ATT TCC TAC AAT TAT GAT TAC TAT ATC CGA GGA GCA ACA ACC ACT TTC TCT GCA GTG GAA AGG GAT CGC CAG TGG AAG TTC ATG humano ATG TGC CGG ATG ACT GAA TAC GAC TGT GAA TTT GCA AAT GTT TAG Fig. 1C ou um seu fragmento? b) se transformar uma célula hospedeira com o citado vector e; c) se cultivarem as células transformadas resultantes em condições em que se expressa o péptido codificado pela referida sequência de ADN ou pelo seu fragmento. 2-. - Processo para a preparaçao de factor de calcificação óssea, caracterizado pelo facto de compreender as operações que consistem em a) se construir um vector que inclui a seguinte sequência de ADN bovino CAG TAT GGT GAC TAT GGG TAC TCC TAT 33, -Bovino CAT CAG TAC CAT GAC TAC AGT GAC GAT GGG TGG GTG AAT CTG AAC CGG CAG GGC TTC AGC TAC CAG TGT CCC CAC GGG CAG GTG GTG GTG GCC GTG Bovino AGG AGC ATC TTC AAC AAG AAG GAA GGT TCC GAC AGA CAG TGG ACC TAC GCC TGC ATG CCC ACA CCC CAG AGC CTG GGG GAG CCT ACG GAG TGC TGG Bovino TGG GAG GAG ATC AAC AGG GCT GGA ATG GAA TGG TAC CAG ACA TGC TCC AAC AAT GGA CTG GTG GCA GGA TTC CAG AGC CGC TAC TTC GAG TCA GTG Bovino CTG GAT CGG GAG TGG CAA TTT TAC TGG TGT CGC TAC AGG AGG AGA TGC CCA TAT TCC TGC TGG CTG ACA ACA GAA TAT CCA GGC CAC TAT GGT GAG Bovino GAG ATG GAC ATG ATT TCC TAC AAT TAT GAT TAC TAT ATG CGA GGG GCA ACA ACC ACT TTC TCT GCA GTG GAA AGG GAT CGC CAG TGG AAA TTC AT Bovino ATG TGC CGG ATG ACT GAC TAT GAC TGT GAA TTT GAC AAT GTT TAG Fig. 1D ou um seu fragmento de iniciação de calcificação; b) se transformar uma célula hospedeira com o referido vector; e c) se cultivarem as células transformadas resultantes em condições em que se expressa o péptido codificado pela citada sequência de ADN ou por um seu fragmento. 3-. - Processo de acordo com a reivindicação 1, caracterizado pelo facto de a mencionada sequência de ADN compreender ainda uma sequência 5 escolhida do grupo constithido_.pela sequência principal ATG, GAC, CTC AGT CTT CTC TGGGTA CTT CTG CCC CTA GTC ACC ATG GCC TGG GGC e qualquer sequência derivada por remoção de um ou de vários desoxi-nucleótidos a partir da extremidade 5' da mencionada sequência principal. 4¾. - Processo de acordo com a reivindicação 2, caracterizado pelo facto de a mencionada sequência de nucleótidos de ADN compreender ainda uma sequência 5' escolhida do grupo formado pela sequência principal ATG GAC CTC AGT CTT CTC TGG GTG CTT CTG CCA CTG GTC ACC ATG GCC TGG GGA e qualquer sequência derivada por remoção de um ou de vá-rios desoxinucleótidos a partir da extremidade 5' da referida sequência principal. 5^. - Processo de acordo com qualquer das reivindicações 1 4, caracterizado pelo facto de a citada célula hospedeira ser uma célula eucariótica. 6ã. - Processo de acordo com a reivindicação 5, caracteriza do pelo facto de a citada célula hospedeira compreender uma levedura. 7^. - Processo de acordo com a reivindicação 5, caracteriza do pelo facto de o mencionado vector compreender um promotor GAPDH que controla a expressão do citado pép-tido. J 8^. - Processo de acordo com a reivindicação 5, caracteriza do pelo facto de o^referido promotor ADH2/GAPDH que controla a expressão do referido péptido. 9^. -- Processo de acordo com qualquer das reivindicações anteriores, caracterizado pelo facto de se produzir ADN não cromossómico com a sequência humano CAG TAT GGC GAT TAT GGA TAC CCA TAC humano CAG CAG TAT CAT GAC TAC AGC GAT GAT GGG TGG GTG AAT TTG AAC CGG CAA GGC TTC AGC TAC CAG TGT CCC CAG GGG CAG GTG ATA GTG GCC GTG humano AGG AGC ATC TTC AGC AAG AAG GAA GGT TCT GAC AGA CAA TGG AAC TAC GCC TGC ATG CCC ACG CCA CAG AGC CTC GGG GAA CCC ACG GAG TGC TGG humano TGG GAG GAG ATC AAC AGG GCT GGC ATG GAA TGG TAC CAG ACG TGC TCC AAC AAT GGG CTG GTG GCA GGA TTC CAG AGC GGC TAC TTC GAG TCA GTG humano CTG GAT CGG GAG TGG CAG TTT TAC TGT TGT CGC TAC AGC AAG AGA TGC CCA TAT TCC TGC TGG CTA ACA ACA GAA TAT CCA GGT CAC TAT GGT GA humano GAG ATG GAC ATG ATT TCC TAC AAT TAT GAT TAC TAT ATC CGA GGA GCA ACA ACC ACT TTC TCT GCA GTG GAA AGG GAT CGC CAG TGG AAG TTC ATC humano ATG TGC CGG ATG ACT GAA TAC GAC TGT GAA TTT GCA AAT GTT TAG 1C Fig 35 -loa. - Processo de acordo com qualquer das reivindicações 1 a 8 caracterizado pelo facto de se obter ARN complementai da sequência referida na reivindicação 9. J - Processo de acordo com qualquer das reivindicações 1 a 8, caracterizado pelo facto de se produzir ADN nao cro mossómico com a sequência Bovino CAG TAT GGT GAC TAT GGG TAC TCC TAT Bovino CAT CAG TAC CAT GAC TAC AGT GAC GAT GGG TGG GTG ΔΑΤ CTG AAC CGG CAG GGC TTC AGC TAC CAG TGT CCC CAC GGG CAG GTG GTG GTG GCC GTG Bovino AGG AGC ATC TTC AAC AAG AAG GAA GGT TCC GAC AGA CAG AGG AGC TAC GCC TGC ATG CCC ACA CCC CAG AGC CTG GGG GAG CCT ACG GAG TGC TGG Bovino TGG GAG GAG ATC AAC AGG GCT GGA ATG GAA TGG TAC CAG ACA TGC TCC AAC AAT GGA CTG GTG GCA GGA TTC CAG AGC CGC TAC TTC GAG TCA GTG Bovino CTG GAT CGC GAG TGG CAA TTT TAC TGC TGT CGC TAC AGC AAG AGA TGC CCA TAT TCC TGC TGG CTG ACA ACA GAA TAT CCA GGC CAC TAT GGT GAG Bovino GAG ATG GAC ATG ATT TCC TAC AAT TAT GAT TAC TAT ATG CGA GGG GCA ACA ACC ACT TTC TCT GCA GTG GAA AGG GAT CGC CAG TGG AAA TTC AT Bovino ATG TGC CGG ATG ACT GAC TAT GAC TGT GAA TTT GCA AAT GTT TAG Fig. . 1D 12a. - Processo de acordo com qualquer das reivindicações 1 a 8, caracterizado pelo facto de se obter ADN complementar da sequência referida na reivindicação 11. 13-. J - Processo de acordo com a reivindicação 9, caracterizado pelo facto de se obter ADN não cromossómico que compreende ainda a sequência 5' escolhida do grupo constituído pela sequência principal ATG GAC CTC AGT CTT CTC TGG GTA CTT CTG CCC CTA GTC ACC ATG GCC TGG GGC e -Se-quências derivadas por remoção de um ou de vários deso-xinucleótidos a partir da extremidade 5' da mencionada sequência principal. - Processo de acordo com a reivindicação 11, caracterizado pelo facto de se obter ADN não cromossómico que compreende ainda a sequência 5' escolhida do grupo formado pela sequência principal ATfíPGAC CTC ACT CTT CTG TGG GTG CTT CTG CCA CTG GTC ACC GTG GCT TGG GGA:e..sequêneias derivadas por remoção de-um ou vários desoxinucleótidos a. 14¾.partir da extremidade 5' da mencionada sequência principal . 15ã _ processo de acordo com qualquer das reivindicações 1 a 8, caracterizado pelo facto de se obter um vector replicá-vel que compreende ADN de acordo com a reivindicação 9. 16â - Processo de acordo com qualquer das reivindicações 1 a 8, caracterizado pelo facto de se obter um vector replicá-vel compreendendo ADN de acordo com a reivindicação 11. 175 _ Processo de acordo com qualquer das reivindicações 1 a 8, caracterizado pelo facto de se obter um vector replicá-vel compreendendo ADN de acordo com a reivindicação 14. 18â - Processo de acordo com qualquer das reivindicações 1 a 8, caracterizado pelo facto de se obter um vector replicá-vel compreendendo ADN de acordo com a reivindicação 14. 19^ - processo de acordo com qualquer das reivindicações 1 a 8, caracterizado pelo facto de se obter células de um hospedeiro transformadas com um vector replicável de acorde com a reivindicação 15. 20¾ - Processo de acordo com qualquer das reivindicações 1 a 8, caracterizado pelo facto de se obter células de um hospedeiro transformadas com um vector replicável de acordo com a reivindicação 16. 21¾ - Processo de acordo com qualquer das reivindicações 1 a 8, caracterizado pelo facto de se obter células de um hospedeiro transformadas com um vector replicável de acordo com a reivindicação 17. 22¾ - Processo de acordo com qualquer das reivindicações 1 a 8, caracterizado pelo facto de se obter células de um hospe deiro transformadas com um vector replicável de acordo com a reivindicação 18. 23a - Processo para a preparação de composições farmacêuticas caracterizado pelo facto fe se misturar um polipéptido - 37 - /1 - 37 - /1 // 24a. 25¾. 26a. /P,í escolhidos do grupo que consiste em factor de calcificação óssea (BCF) de mamíferos e seus análogos substar. cialmente isentos de outros factores osteoindutores.azs sociados, preparados de acordo com qulaquer das reivir. dicações anteriores, com as substâncias veiculares e auxiliares farmacêuticamente aceitáveis. Processo de acordo com a reivindicação 23, caracteri-zado pelo facto de o referido factortde calcificação óssea de mamíferos ser BCF humano. Processo de acordo com a reivindicação 23, caracteri-zado pelõ facto de o citado factor de calcificação óssea de mamíferos ser BCF bovino. Processo de acordo com a reivindicação 24, caracteris zado pelo facto de o mencionado polipeptido compreender uma sequência de aminoácidos como se segue humano GLN TYR GLY ASP TYR humano GLN GLN PIR HIS ASP VAL ASN LEU ASN ARG GYS PRO GLN GLY GLN humano ARS SER ILE PHE SER ARG GLY TRP ASN TYR GLN SER LEU GLY GLU humano TRP GLU GLU ILE ASN TYR SLN THR CYS SER GLY PHE GLN SER ARG humano LEU ASP ARG GLU TRP TYR SER LYS ARG CYS THR THR GLU TYR PRO humano GLU MET ASP MET ILE PYR ILE ARG GLY ALA VAL GLU ARG ASP ARG humano MET CYS ARG MET THR ALA ASN VAL Fig. IA GLY TYR PRO TYR TYR SER ASP ASP GLY TRP GLN GLY LEU SER TYR GLN VAL ILE VAL ALA VAL LYS LYS GLU GLY SER ASP ALA GYS TET PRO TAR PRO PRO THR GLU GYS TRP ARG ALA GLY MET GLU TRP ASN ASN ELY LEU VAL ALA TYR PHE GLU SER VAL GLN PHE TYR CYS CYS ARG PRO TYR SER CYS TRP LEU GLY HIS TYR GLY GL SER PYR ASN TYR ASP PYR THR THR THR PHE SER ALA GLN TRP LYS PHE ILE GLU TYR ASP CYS GLU PHE ou um seu fragmento. Processo de acordo com a reivindicação 25, caracteri-zado pelo facto de o mencionado polipeptido compreender a seguinte sequência de aminoácidos Bovino GLN TYR GLY ASP TIR GLY TYR SER TYR Bovino HIS GLN TYR HIS ASP TYR SER ASP ASP GLY TRP VAL ASN LEU ASN ARG GLN GLY LEU SER TYR GLN CYS PRO HIS GLY GLN VAL VAL VAL ALA VAL 27®.Bovino a g: SER ILE ASN LYS LYS GLU GLY SER ASP ARG ELN TRP ASN TYR ALA CYS MET PRO THR PRO GLN SER LEU GLY GLU PRO THR GLU CYS TRF Bovino TRP GLU GLU ILE ASN ARG ALA GLY MET GLU TRP TYR GLN THR CYS SER ASN ASN GLY LEU VAL ALA GLY PHE GLN SER ARG TYR PHE GLU SER VAL Bovino LEU ASP ARG GLU TRP GLN PHE TYR CYS CYS ARG TYR SER LYS ARG SYS PRO TYR SER CYS TRP LEU THR THR GLU TYR PRO GLY HIS TYR GLY GL Bovino GLU MET ASP MET ILE SER TYR ASN TYR ASP TYR TYR MET ARG GLY ALA THR THR THR PHE SER ALA VAL GLU ARG ASP ARG GLN TRP LYS PHE Bovino MET CYS ARG MET THR ASP TYR ASP CYS GLU THE ALA ASN VAL Fig. 1B J ou um seu fagmento. 28^. - Processo de acordo com a reivindicação 26, caracteri-zado pelo facto de o citado polipéptido compreender uma extremidade amino escolhida do grupo formado pela sequência de péptido de sinal met-asp-leu-ser-leu-leu-trp-val-leu-leu-pro-leu-val-thr-met-ala-trp-gly- e sequências da citada sequência de péptido de sinal derivadas por meio da anulação de um ou de vários amino-ácidos da extremidade amino da referida sequência de péptido de sinal. J 29â. - Processo de acordo com a reivindicação 27, caracteriza-do pelo facto de o mencionado polipéptido compreender uma extremidade amino escolhida do grupo formado pela sequência de péptido de sinal met-asp-leu-thr-leu-leu--trp- val-leu-leu-pro-leu-val-thr-val-ala-trp-gly e sequências da referida sequência de péptido de sinal, derivadas por remoção de um ou vários aminoácidos da extremidade amino da citada sequência de péptido de sinal. 30â. - Processo para a preparação de uma composição farmacêutica que provoca a calcificação, caracterizado pelo faç to de se misturar^uma quantidade de uma mistura de faç tor de calcificação óssea de mamíferos, ou um seu análogo com uma proteína Gla de matriz. . - Processo de acordo com a reivindicação 30, caracterizado pelo facto de o citado factor compreender o fac-tor de calcificação óssea humano. 31*u - 32a. 33^. J 34^. J - Processo de acordo com a reivindicação 30, caracteriza-do pelo facto^de o citado factor compreender o factor de calcificação óssea bovina. Processo de acordo com a reivindicação 31, caracteriza- do pelo facto de 0 citado factor possuir a seguinte sequência de amindacidos humano GUI TYR GLY ASP TYR GLY TYR PRO TYR humano GIN GLN TYR HIS ASP TYR SER ASP ASP GLY TRP VAL ASN LEU ASN ARG GLN GLY LEU SER TYR GLN CYS PRO GLN GLT GLN VAL ILE VAL ALA VAL humano ARS SER ILE PHE SER LYS LYS GLU GLY SER ASP ARG GLN TRP ASN TYR ALA CYS TET PRO THR PRO GLN SER LEU GLY GLU PRO THR GLU CYS TRP humano TRP GLU GLU ILE ASN ARG ALA GLY MET GLU TRP TYR SLN THR CYS SER ASN ASN GLY LEU VAL ALA GLY PHE GLN SER ARG TYR PHE GLU SER VAL humano LEU ASP ARG GLU TRP GLN PHE TYR CYS CYS ARG TYR SER LYS ARG CYS PRO TYR SER CYS TRP LEU THR THR GLU TYR PRO GLY HIS TYR GLY GL humano GLU MET ASP MET ILE SER TYR ASN TYR ASP TYR TYR ILE ARG GLY ALA THR THR THR PHE SER ALA VAL GLU ARG ASP ARG GLN TRP LYS PHE ILE humano MET CYS ARG MET THR GLU TYR ASP CYS GLU PHE ALA ASN VAL Pig. IA ou um seu fragmento Processo de acordo com a reivindicação 32, caracteri- zado pelo facto de 0 referido factor ter a seguinte sequencia aminoacido Bovino GLN TYR GLY ASP TYR GLY TYR SER TYR Bovino HIS GLN TYR HIS ASP TYR SER ASP ASP GLY TRP VAL ASN LEU ASN ARG GLN GLY LEU SER TYR GLN CYS PRO HIS GLY GLN VAL VAL VAL VAL VAL Bovino AAG SER ILE PHE ASN LYS LYS GLU GLY SER ASP ARG ELN TRP ASN TYR ALA CYS MET PRO THR PRO GLN SER LEU GLY GLU PRO THR GLU CYS TRP Bovino TRP GLU GLU ILE ASN ARG ALA GLY MET GLU TRP TYR GLN TYH CYS SER ASN ASN GLY LEU VAL ALA GLY PHE GLN SER ARG TYR PHE GLU SER VAL Bovino LEU ASP ARG GLU TRP GLN PHE TYR CYS CYS ARG TYR SER LYS ARG CYS PRO TYR SER CYS TRP LEU TRH TRH GLU TYR PRO GLY HIS TYR GLY GL Bovino GLU MET ASP MET ILE SER TYR ASN TYR ASP TYR TYR MET ARG GLY ALA THR THR THR PHE SER ALA VAL GLU40ti ARG ASP AFG GLN TRP LYS PHE Bovino MET CYS ARG MET THR ASP TYR ASP CYS GLU PHE ALA ASN VAL Fig, 1B ou um seu fragmento.
- 353 - Processo para a preparação de composições para reconhecer um único epítopo para o factor de calcificação óssea de mamíferos, caracterizado pelo facto des e misturarem an-ti-corpos que reconhecem o referido epítopo com as substâncias auxiliares e veiculares farmacêuticamente aceita veis. * ™ 36¾ - Processo para provocar a calcificação para a formação de tecido ósseo num vertebrado, caracterizado pelo facto de se administrar ao referido vertebrado, de uma maneira farmacêuticamente eficaz, uma quantidade^efectiva, para provocar a calcificação, de uma composição de acordo com qualquer das reivindicações 30 a 34, de preferência, com preendida entre cerca de 0,1 micrograma e cerca de 100 miligramas por kilograma de peso corporal. | 37a - Processo de diagnóstico, caracterizado pelo facto de com preender as operações que consistem em se obter uma amos tra de osso de um mamífero, e se medir a quantidade de | factor de calcificação óssea existente na mencionada amo£i tra mediante um ensaio quantitativo. jisboa, O Agente Oficial da Propriedade IndustrialAgente Oficial de Prcpriadade Industria! R. Casííilio. 201-S. £.-1000 LISBOA Telefs. 65 13 39 - 65 46 13
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US36082689A | 1989-06-02 | 1989-06-02 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| PT94241A true PT94241A (pt) | 1991-02-08 |
Family
ID=23419550
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PT94241A PT94241A (pt) | 1989-06-02 | 1990-06-01 | Processo para a preparacao de factor calcificacao ossea e de composicoes farmaceuticas que os contem |
Country Status (4)
| Country | Link |
|---|---|
| US (1) | US5635374A (pt) |
| EP (1) | EP0401055A3 (pt) |
| JP (1) | JPH03151877A (pt) |
| PT (1) | PT94241A (pt) |
Families Citing this family (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6150328A (en) | 1986-07-01 | 2000-11-21 | Genetics Institute, Inc. | BMP products |
| ATE238417T1 (de) | 1991-11-04 | 2003-05-15 | Inst Genetics Llc | Rekombinante knochenmorphogenetische protein heterodimere, zusammensetzungen und verfahren zur verwendung |
| DE69224741T2 (de) * | 1991-12-26 | 1998-07-02 | Snow Brand Milk Prod Co Ltd | Die knochen stärkender faktor und lebensmittel und getränke die diesen faktor enthalten |
| US6291206B1 (en) | 1993-09-17 | 2001-09-18 | Genetics Institute, Inc. | BMP receptor proteins |
| AU689184B2 (en) | 1993-12-07 | 1998-03-26 | Genetics Institute, Llc | BMP-12, BMP-13 and tendon-inducing compositions thereof |
| US6727224B1 (en) | 1999-02-01 | 2004-04-27 | Genetics Institute, Llc. | Methods and compositions for healing and repair of articular cartilage |
| DE60012557T2 (de) | 1999-10-15 | 2005-08-04 | Genetics Institute, LLC, Cambridge | Hyaluronsäure enthaltende zusammensetzungen zur abgabe osteogener proteine |
| CA2449008A1 (en) | 2001-06-01 | 2002-12-12 | Wyeth | Compositions and methods for systemic administration of sequences encoding bone morphogenetic proteins |
| TWI267378B (en) | 2001-06-08 | 2006-12-01 | Wyeth Corp | Calcium phosphate delivery vehicles for osteoinductive proteins |
| EP1772154A3 (en) | 2003-09-12 | 2011-09-07 | Wyeth LLC | Injectable calcium phosphate pastes for delivery of osteogenic proteins |
Family Cites Families (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4455256A (en) * | 1981-05-05 | 1984-06-19 | The Regents Of The University Of California | Bone morphogenetic protein |
| US4761471A (en) * | 1980-08-04 | 1988-08-02 | The Regents Of The University Of California | Bone morphogenetic protein composition |
| US4619989A (en) * | 1981-05-05 | 1986-10-28 | The Regents Of The University Of Cal. | Bone morphogenetic protein composition |
| US4294753A (en) * | 1980-08-04 | 1981-10-13 | The Regents Of The University Of California | Bone morphogenetic protein process |
| US4394370A (en) * | 1981-09-21 | 1983-07-19 | Jefferies Steven R | Bone graft material for osseous defects and method of making same |
| US4434094A (en) * | 1983-04-12 | 1984-02-28 | Collagen Corporation | Partially purified osteogenic factor and process for preparing same from demineralized bone |
| US4795804A (en) * | 1983-08-16 | 1989-01-03 | The Regents Of The University Of California | Bone morphogenetic agents |
| US4804744A (en) * | 1984-01-04 | 1989-02-14 | International Genetic Engineering, Inc. | Osteogenic factors |
| NZ210699A (en) * | 1984-01-04 | 1989-06-28 | Int Genetic Eng | Isolation of an osteogenic protein of the p3 immunologically related family |
| US4526909A (en) * | 1984-01-09 | 1985-07-02 | Regents Of The University Of California | Polymethylmethacrylate delivery system for bone morphogenetic protein |
| US4563489A (en) * | 1984-02-10 | 1986-01-07 | University Of California | Biodegradable organic polymer delivery system for bone morphogenetic protein |
| US4596574A (en) * | 1984-05-14 | 1986-06-24 | The Regents Of The University Of California | Biodegradable porous ceramic delivery system for bone morphogenetic protein |
| JPS60253455A (ja) * | 1984-05-28 | 1985-12-14 | 京セラ株式会社 | 骨形成因子を含有する生体材料とその製造方法 |
| ATE128715T1 (de) * | 1984-07-16 | 1995-10-15 | Celtrix Pharma | Polypeptide induzierende faktoren in knochen und knorpel. |
| US4627982A (en) * | 1984-07-16 | 1986-12-09 | Collagen Corporation | Partially purified bone-inducing factor |
| DE3679343D1 (de) * | 1985-03-28 | 1991-06-27 | Chiron Corp | Expression durch verwendung von fusionsgenen fuer proteinproduktion. |
| JPH068318B2 (ja) * | 1985-07-08 | 1994-02-02 | セルトリックス ファーマシューティカルズ,インコーポレイテッド | 部分精製骨誘導因子 |
| IL83003A (en) * | 1986-07-01 | 1995-07-31 | Genetics Inst | Osteoinductive factors |
| ATE112684T1 (de) * | 1987-04-28 | 1994-10-15 | Boehringer Mannheim Gmbh | Verwendung von igf-ii zur behandlung von knochenkrankheiten. |
| EP0336760A3 (en) * | 1988-04-06 | 1991-03-13 | Celtrix Pharmaceuticals, Inc. | Bone-inducing protein |
| US5106626A (en) * | 1988-10-11 | 1992-04-21 | International Genetic Engineering, Inc. | Osteogenic factors |
| US5051255A (en) * | 1988-10-14 | 1991-09-24 | Abbott Laboratories | Nematocidal preparations |
-
1990
- 1990-06-01 PT PT94241A patent/PT94241A/pt not_active Application Discontinuation
- 1990-06-01 JP JP2145256A patent/JPH03151877A/ja active Pending
- 1990-06-04 EP EP19900306058 patent/EP0401055A3/en not_active Ceased
-
1994
- 1994-05-04 US US08/237,243 patent/US5635374A/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| EP0401055A3 (en) | 1991-08-07 |
| US5635374A (en) | 1997-06-03 |
| JPH03151877A (ja) | 1991-06-28 |
| EP0401055A2 (en) | 1990-12-05 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| KR100393508B1 (ko) | 인간 인터루킨 4의 안타고니스트 또는 부분적 아고니스트로서의 신규hIL-4 변이단백질 | |
| Cooke et al. | Two distinct species of human growth hormone-variant mRNA in the human placenta predict the expression of novel growth hormone proteins. | |
| Sage et al. | Characterization of a novel collagen chain in human placenta and its relation to AB collagen | |
| CA2215394A1 (en) | Il-17 receptor | |
| KR20010032147A (ko) | 단쇄상 이작용기성 당단백질 호르몬 | |
| KR890700610A (ko) | 백혈병 억제 인자 | |
| PT94241A (pt) | Processo para a preparacao de factor calcificacao ossea e de composicoes farmaceuticas que os contem | |
| WO1998024811A2 (en) | Vascular endothelial growth factor | |
| CA2030108C (en) | Process for the preparation of genetic vectors for the expression of nerve growth factor in eukaryotic cells | |
| JP2525048B2 (ja) | 部位特異的変異形成で修飾された糖蛋白質ホルモンおよびその使用 | |
| US6180602B1 (en) | Human novel cDNA, TGF-beta superfamily protein encoded thereby and the use of immunosuppressive agent | |
| Proost et al. | Chemical synthesis, purification and folding of the human monocyte chemotactic proteins MCP-2 and MCP-3 into biologically active chemokines | |
| DE69636052T2 (de) | Mpl-liganden analoga | |
| TSURU et al. | Isolation and amino acid sequence of a peptide containing an epoxide-reactive residue from the thermolysin-digest of Scytalidium lignicolum acid protease B | |
| KR920012440A (ko) | 인간 인터류킨-5 수용체 | |
| WO1997023616A1 (de) | Polypeptide mit il-16-aktivität, verfahren zu ihrer herstellung und verwendung | |
| DE68906932T2 (de) | Verfahren zur reinigung und isolierung carboxyl-endstaendiger peptide. | |
| Barone et al. | The expression in Escherichia coli of recombinant human platelet factor 4, a protein with immunoregulatory activity. | |
| EP0107710A1 (en) | The manufacture and expression of genes for calcitonin and polypeptide analogs thereof | |
| Li et al. | Cancer-associated lactate dehydrogenase is a tyrosylphosphorylated form of human LDH-A, skeletal muscle isoenzyme | |
| DE19611234C1 (de) | Tyrosin-Phosphatase-verwandtes Protein | |
| DE69323465T2 (de) | Sulfatase-ähnliches Protein aus Knochen und Verfahren zu dessen Herstellung | |
| US6756357B1 (en) | Variants of human ciliary neurotrophic factor (hCNTF) | |
| EP0904374A1 (de) | Prozessierte polypeptide mit il-16-aktivität, verfahren zu ihrer herstellung und verwendung | |
| WO1994023024A1 (en) | Dna encoding cobra c3, cvf1, and cvf2 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FC3A | Refusal |
Effective date: 19960305 |