AU712575B2 - Peptides which bind to prothrombin and thrombin - Google Patents
Peptides which bind to prothrombin and thrombin Download PDFInfo
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- AU712575B2 AU712575B2 AU26220/97A AU2622097A AU712575B2 AU 712575 B2 AU712575 B2 AU 712575B2 AU 26220/97 A AU26220/97 A AU 26220/97A AU 2622097 A AU2622097 A AU 2622097A AU 712575 B2 AU712575 B2 AU 712575B2
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- thrombin
- peptide
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- gly
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- DVLWZWNAQUBZBC-ZNSHCXBVSA-N Val-Thr-Pro Chemical compound C[C@H]([C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](C(C)C)N)O DVLWZWNAQUBZBC-ZNSHCXBVSA-N 0.000 description 1
- 229930003448 Vitamin K Natural products 0.000 description 1
- QWXOJIDBSHLIFI-UHFFFAOYSA-N [3-(1-chloro-3'-methoxyspiro[adamantane-4,4'-dioxetane]-3'-yl)phenyl] dihydrogen phosphate Chemical compound O1OC2(C3CC4CC2CC(Cl)(C4)C3)C1(OC)C1=CC=CC(OP(O)(O)=O)=C1 QWXOJIDBSHLIFI-UHFFFAOYSA-N 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 229960003767 alanine Drugs 0.000 description 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 150000001447 alkali salts Chemical class 0.000 description 1
- WLDHEUZGFKACJH-UHFFFAOYSA-K amaranth Chemical compound [Na+].[Na+].[Na+].C12=CC=C(S([O-])(=O)=O)C=C2C=C(S([O-])(=O)=O)C(O)=C1N=NC1=CC=C(S([O-])(=O)=O)C2=CC=CC=C12 WLDHEUZGFKACJH-UHFFFAOYSA-K 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- 239000002506 anticoagulant protein Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 108010062796 arginyllysine Proteins 0.000 description 1
- 238000003149 assay kit Methods 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 239000003114 blood coagulation factor Substances 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 230000035602 clotting Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- AGVAZMGAQJOSFJ-WZHZPDAFSA-M cobalt(2+);[(2r,3s,4r,5s)-5-(5,6-dimethylbenzimidazol-1-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2r)-1-[3-[(1r,2r,3r,4z,7s,9z,12s,13s,14z,17s,18s,19r)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2 Chemical compound [Co+2].N#[C-].[N-]([C@@H]1[C@H](CC(N)=O)[C@@]2(C)CCC(=O)NC[C@@H](C)OP(O)(=O)O[C@H]3[C@H]([C@H](O[C@@H]3CO)N3C4=CC(C)=C(C)C=C4N=C3)O)\C2=C(C)/C([C@H](C\2(C)C)CCC(N)=O)=N/C/2=C\C([C@H]([C@@]/2(CC(N)=O)C)CCC(N)=O)=N\C\2=C(C)/C2=N[C@]1(C)[C@@](C)(CC(N)=O)[C@@H]2CCC(N)=O AGVAZMGAQJOSFJ-WZHZPDAFSA-M 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000010511 deprotection reaction Methods 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 238000011067 equilibration Methods 0.000 description 1
- 102000034356 gene-regulatory proteins Human genes 0.000 description 1
- 108091006104 gene-regulatory proteins Proteins 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- KZNQNBZMBZJQJO-YFKPBYRVSA-N glyclproline Chemical compound NCC(=O)N1CCC[C@H]1C(O)=O KZNQNBZMBZJQJO-YFKPBYRVSA-N 0.000 description 1
- 108010077515 glycylproline Proteins 0.000 description 1
- 230000002439 hemostatic effect Effects 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 229940127121 immunoconjugate Drugs 0.000 description 1
- 239000000543 intermediate Substances 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 230000036457 multidrug resistance Effects 0.000 description 1
- ANORDWOIBSUYBN-UHFFFAOYSA-N n-chloro-1-phenylmethanamine Chemical compound ClNCC1=CC=CC=C1 ANORDWOIBSUYBN-UHFFFAOYSA-N 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- SHUZOJHMOBOZST-UHFFFAOYSA-N phylloquinone Natural products CC(C)CCCCC(C)CCC(C)CCCC(=CCC1=C(C)C(=O)c2ccccc2C1=O)C SHUZOJHMOBOZST-UHFFFAOYSA-N 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 150000003141 primary amines Chemical class 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 108010014614 prolyl-glycyl-proline Proteins 0.000 description 1
- 108010079317 prolyl-tyrosine Proteins 0.000 description 1
- 125000006239 protecting group Chemical group 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 229940024790 prothrombin complex concentrate Drugs 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 239000001044 red dye Substances 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 239000000565 sealant Substances 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 239000003001 serine protease inhibitor Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 239000012622 synthetic inhibitor Substances 0.000 description 1
- 108010031354 thermitase Proteins 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 235000019168 vitamin K Nutrition 0.000 description 1
- 239000011712 vitamin K Substances 0.000 description 1
- 150000003721 vitamin K derivatives Chemical class 0.000 description 1
- 150000003722 vitamin derivatives Chemical class 0.000 description 1
- 229940046010 vitamin k Drugs 0.000 description 1
- PJVWKTKQMONHTI-UHFFFAOYSA-N warfarin Chemical compound OC=1C2=CC=CC=C2OC(=O)C=1C(CC(=O)C)C1=CC=CC=C1 PJVWKTKQMONHTI-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
-
- 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
- C07K14/745—Blood coagulation or fibrinolysis 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6429—Thrombin (3.4.21.5)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21005—Thrombin (3.4.21.5)
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Medicinal Chemistry (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Hematology (AREA)
- Microbiology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
- Saccharide Compounds (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/672,805 US5831003A (en) | 1996-06-28 | 1996-06-28 | Peptides which bind to prothrombin and thrombin |
| US08/672805 | 1996-06-28 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU2622097A AU2622097A (en) | 1998-01-15 |
| AU712575B2 true AU712575B2 (en) | 1999-11-11 |
Family
ID=24700072
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU26220/97A Ceased AU712575B2 (en) | 1996-06-28 | 1997-06-23 | Peptides which bind to prothrombin and thrombin |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US5831003A (enExample) |
| EP (1) | EP0816377B1 (enExample) |
| JP (1) | JP3978258B2 (enExample) |
| AT (1) | ATE215964T1 (enExample) |
| AU (1) | AU712575B2 (enExample) |
| CA (1) | CA2206663A1 (enExample) |
| DE (1) | DE69711765T2 (enExample) |
| DK (1) | DK0816377T3 (enExample) |
| ES (1) | ES2175218T3 (enExample) |
| PT (1) | PT816377E (enExample) |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6462180B1 (en) * | 1999-11-24 | 2002-10-08 | Bayer Corporation | Method of preparing α-1 proteinase inhibitor |
| EP1343809B2 (en) | 2000-12-14 | 2023-03-15 | Grifols Therapeutics Inc. | Method of preparing alpha-1 proteinase inhibitor |
| GB0211849D0 (en) * | 2002-05-23 | 2002-07-03 | Mok Kenneth H | Improvments to retro-inverso isomers |
| FR2884418B1 (fr) * | 2005-04-15 | 2008-11-21 | Soc Extraction Principes Actif | Utilisation d'un peptide comme principe actif amincissant |
| EP2502628B1 (en) | 2006-06-23 | 2016-12-14 | Alethia Biotherapeutics Inc. | Polynucleotides and polypeptide sequences involved in cancer |
| WO2010060186A1 (en) | 2008-11-03 | 2010-06-03 | Alethia Biotherapeutics Inc. | Antibodies that specifically block the biological activity of a tumor antigen |
| US8945895B2 (en) | 2009-07-31 | 2015-02-03 | Baxter International Inc. | Methods of purifying recombinant ADAMTS13 and other proteins and compositions thereof |
| DK3173427T3 (da) | 2011-03-31 | 2019-08-05 | Adc Therapeutics Sa | Antistoffer mod nyre-associeret antigen 1 og antigen-bindende fragmenter deraf |
| HRP20190946T1 (hr) | 2012-01-09 | 2019-07-26 | Adc Therapeutics Sa | Sredstva za liječenje trostruko negativnog raka dojke |
| EP3262409B1 (en) | 2015-02-25 | 2020-03-25 | Omrix Biopharmaceuticals Ltd. | Method for purifying and quantifying thrombin and its degradation polypeptides |
| ES2791982T3 (es) * | 2015-02-25 | 2020-11-06 | Omrix Biopharmaceuticals Ltd | Método para purificar y cuantificar la trombina y sus polipéptidos de degradación |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA1341032C (en) * | 1987-01-23 | 2000-06-20 | John L. Krstenansky | Anticoagulant peptides |
| US5367060A (en) * | 1991-05-24 | 1994-11-22 | Genentech, Inc. | Structure, production and use of heregulin |
-
1996
- 1996-06-28 US US08/672,805 patent/US5831003A/en not_active Expired - Lifetime
-
1997
- 1997-06-16 ES ES97109744T patent/ES2175218T3/es not_active Expired - Lifetime
- 1997-06-16 AT AT97109744T patent/ATE215964T1/de active
- 1997-06-16 DE DE69711765T patent/DE69711765T2/de not_active Expired - Lifetime
- 1997-06-16 DK DK97109744T patent/DK0816377T3/da active
- 1997-06-16 PT PT97109744T patent/PT816377E/pt unknown
- 1997-06-16 EP EP97109744A patent/EP0816377B1/en not_active Expired - Lifetime
- 1997-06-23 AU AU26220/97A patent/AU712575B2/en not_active Ceased
- 1997-06-24 JP JP18189597A patent/JP3978258B2/ja not_active Expired - Fee Related
- 1997-06-25 CA CA002206663A patent/CA2206663A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| CA2206663A1 (en) | 1997-12-28 |
| DE69711765T2 (de) | 2002-10-02 |
| PT816377E (pt) | 2002-08-30 |
| DK0816377T3 (da) | 2002-07-22 |
| DE69711765D1 (de) | 2002-05-16 |
| JP3978258B2 (ja) | 2007-09-19 |
| EP0816377B1 (en) | 2002-04-10 |
| EP0816377A2 (en) | 1998-01-07 |
| EP0816377A3 (en) | 1998-07-15 |
| AU2622097A (en) | 1998-01-15 |
| ATE215964T1 (de) | 2002-04-15 |
| US5831003A (en) | 1998-11-03 |
| JPH1075778A (ja) | 1998-03-24 |
| ES2175218T3 (es) | 2002-11-16 |
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