NO792553L - Analytiske fluorogene substrater for proteolytiske enzymer - Google Patents
Analytiske fluorogene substrater for proteolytiske enzymerInfo
- Publication number
- NO792553L NO792553L NO792553A NO792553A NO792553L NO 792553 L NO792553 L NO 792553L NO 792553 A NO792553 A NO 792553A NO 792553 A NO792553 A NO 792553A NO 792553 L NO792553 L NO 792553L
- Authority
- NO
- Norway
- Prior art keywords
- arg
- mna
- phe
- gly
- cbz
- Prior art date
Links
- 108091005804 Peptidases Proteins 0.000 title claims description 14
- 102000035195 Peptidases Human genes 0.000 title claims description 13
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 title claims description 6
- 239000007850 fluorescent dye Substances 0.000 title claims 2
- 239000000758 substrate Substances 0.000 claims description 26
- 108090000790 Enzymes Proteins 0.000 claims description 23
- 102000004190 Enzymes Human genes 0.000 claims description 23
- 150000001875 compounds Chemical class 0.000 claims description 23
- 230000000694 effects Effects 0.000 claims description 23
- 229940088598 enzyme Drugs 0.000 claims description 23
- 238000000034 method Methods 0.000 claims description 22
- 108090000190 Thrombin Proteins 0.000 claims description 17
- 229960004072 thrombin Drugs 0.000 claims description 16
- 239000001257 hydrogen Substances 0.000 claims description 11
- 229910052739 hydrogen Inorganic materials 0.000 claims description 11
- 230000005284 excitation Effects 0.000 claims description 9
- 108010088842 Fibrinolysin Proteins 0.000 claims description 8
- 229940012957 plasmin Drugs 0.000 claims description 8
- 108010046645 N-carbobenzoxyglycylproline Proteins 0.000 claims description 7
- HQABUPZFAYXKJW-UHFFFAOYSA-N butan-1-amine Chemical compound CCCCN HQABUPZFAYXKJW-UHFFFAOYSA-N 0.000 claims description 7
- -1 glutaryl Chemical group 0.000 claims description 7
- 125000004432 carbon atom Chemical group C* 0.000 claims description 6
- XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 claims description 6
- 108010068519 N-benzyloxycarbonyl-alanyl-arginyl-arginine 4-methoxy-2-naphthylamide Proteins 0.000 claims description 5
- 239000002253 acid Substances 0.000 claims description 5
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 claims description 5
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 claims description 5
- 108060005987 Kallikrein Proteins 0.000 claims description 4
- 102000001399 Kallikrein Human genes 0.000 claims description 4
- 108010067372 Pancreatic elastase Proteins 0.000 claims description 4
- 102000016387 Pancreatic elastase Human genes 0.000 claims description 4
- 108090000631 Trypsin Proteins 0.000 claims description 4
- 102000004142 Trypsin Human genes 0.000 claims description 4
- 125000003236 benzoyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C(*)=O 0.000 claims description 4
- 125000003170 phenylsulfonyl group Chemical group C1(=CC=CC=C1)S(=O)(=O)* 0.000 claims description 4
- 239000012588 trypsin Substances 0.000 claims description 4
- 235000019260 propionic acid Nutrition 0.000 claims description 3
- IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 claims description 3
- 150000003839 salts Chemical class 0.000 claims description 3
- GNIDSOFZAKMQAO-SECBINFHSA-N (2r)-3-hydroxy-2-(phenylmethoxycarbonylamino)propanoic acid Chemical compound OC[C@H](C(O)=O)NC(=O)OCC1=CC=CC=C1 GNIDSOFZAKMQAO-SECBINFHSA-N 0.000 claims description 2
- DZCCNHQOMASNEB-UHFFFAOYSA-N 1-methoxynaphthalen-2-amine Chemical compound C1=CC=C2C(OC)=C(N)C=CC2=C1 DZCCNHQOMASNEB-UHFFFAOYSA-N 0.000 claims description 2
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 claims description 2
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 claims description 2
- 238000002156 mixing Methods 0.000 claims description 2
- 229960005356 urokinase Drugs 0.000 claims description 2
- 125000004435 hydrogen atom Chemical class [H]* 0.000 claims 6
- 229910052799 carbon Inorganic materials 0.000 claims 3
- OJURWUUOVGOHJZ-UHFFFAOYSA-N methyl 2-[(2-acetyloxyphenyl)methyl-[2-[(2-acetyloxyphenyl)methyl-(2-methoxy-2-oxoethyl)amino]ethyl]amino]acetate Chemical compound C=1C=CC=C(OC(C)=O)C=1CN(CC(=O)OC)CCN(CC(=O)OC)CC1=CC=CC=C1OC(C)=O OJURWUUOVGOHJZ-UHFFFAOYSA-N 0.000 claims 3
- 229910052757 nitrogen Inorganic materials 0.000 claims 3
- 125000004433 nitrogen atom Chemical group N* 0.000 claims 3
- KBZFDRWPMZESDI-UHFFFAOYSA-N 5-aminobenzene-1,3-dicarboxylic acid Chemical compound NC1=CC(C(O)=O)=CC(C(O)=O)=C1 KBZFDRWPMZESDI-UHFFFAOYSA-N 0.000 claims 2
- 150000001721 carbon Chemical group 0.000 claims 2
- 125000006165 cyclic alkyl group Chemical group 0.000 claims 2
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 claims 2
- 239000007788 liquid Substances 0.000 claims 2
- CALBREUZAHFNER-INIZCTEOSA-N (2s)-2-[bis(phenylmethoxycarbonyl)amino]-3-hydroxypropanoic acid Chemical compound C=1C=CC=CC=1COC(=O)N([C@@H](CO)C(O)=O)C(=O)OCC1=CC=CC=C1 CALBREUZAHFNER-INIZCTEOSA-N 0.000 claims 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims 1
- MTCFGRXMJLQNBG-UWTATZPHSA-N D-Serine Chemical compound OC[C@@H](N)C(O)=O MTCFGRXMJLQNBG-UWTATZPHSA-N 0.000 claims 1
- 229930195711 D-Serine Natural products 0.000 claims 1
- NTUPOKHATNSWCY-JYJNAYRXSA-N Phe-Pro-Arg Chemical compound C([C@H](N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O)C1=CC=CC=C1 NTUPOKHATNSWCY-JYJNAYRXSA-N 0.000 claims 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 1
- 238000003776 cleavage reaction Methods 0.000 claims 1
- 125000000896 monocarboxylic acid group Chemical group 0.000 claims 1
- UPSFMJHZUCSEHU-JYGUBCOQSA-N n-[(2s,3r,4r,5s,6r)-2-[(2r,3s,4r,5r,6s)-5-acetamido-4-hydroxy-2-(hydroxymethyl)-6-(4-methyl-2-oxochromen-7-yl)oxyoxan-3-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide Chemical compound CC(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@H]1[C@H](O)[C@@H](NC(C)=O)[C@H](OC=2C=C3OC(=O)C=C(C)C3=CC=2)O[C@@H]1CO UPSFMJHZUCSEHU-JYGUBCOQSA-N 0.000 claims 1
- 108010018625 phenylalanylarginine Proteins 0.000 claims 1
- 230000007017 scission Effects 0.000 claims 1
- 238000005259 measurement Methods 0.000 description 25
- SJRJJKPEHAURKC-UHFFFAOYSA-N N-Methylmorpholine Chemical compound CN1CCOCC1 SJRJJKPEHAURKC-UHFFFAOYSA-N 0.000 description 21
- 229920000669 heparin Polymers 0.000 description 20
- 239000000243 solution Substances 0.000 description 20
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 19
- 229960002897 heparin Drugs 0.000 description 19
- 210000002381 plasma Anatomy 0.000 description 19
- ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 15
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 14
- 102000013566 Plasminogen Human genes 0.000 description 12
- 108010051456 Plasminogen Proteins 0.000 description 12
- 239000000203 mixture Substances 0.000 description 11
- 239000002904 solvent Substances 0.000 description 10
- KDLHZDBZIXYQEI-UHFFFAOYSA-N Palladium Chemical compound [Pd] KDLHZDBZIXYQEI-UHFFFAOYSA-N 0.000 description 9
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 8
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 8
- 239000000523 sample Substances 0.000 description 8
- 239000000872 buffer Substances 0.000 description 7
- 210000004369 blood Anatomy 0.000 description 6
- 239000008280 blood Substances 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 5
- 230000015271 coagulation Effects 0.000 description 5
- 238000005345 coagulation Methods 0.000 description 5
- 239000003112 inhibitor Substances 0.000 description 5
- YOETUEMZNOLGDB-UHFFFAOYSA-N 2-methylpropyl carbonochloridate Chemical compound CC(C)COC(Cl)=O YOETUEMZNOLGDB-UHFFFAOYSA-N 0.000 description 4
- 239000004471 Glycine Substances 0.000 description 4
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 108010023197 Streptokinase Proteins 0.000 description 4
- WYURNTSHIVDZCO-UHFFFAOYSA-N Tetrahydrofuran Chemical compound C1CCOC1 WYURNTSHIVDZCO-UHFFFAOYSA-N 0.000 description 4
- 230000023555 blood coagulation Effects 0.000 description 4
- 210000001124 body fluid Anatomy 0.000 description 4
- 239000010839 body fluid Substances 0.000 description 4
- DEKPYXUDJRABNK-UHFFFAOYSA-N dimethyl 5-aminobenzene-1,3-dicarboxylate Chemical compound COC(=O)C1=CC(N)=CC(C(=O)OC)=C1 DEKPYXUDJRABNK-UHFFFAOYSA-N 0.000 description 4
- 235000019441 ethanol Nutrition 0.000 description 4
- 238000002474 experimental method Methods 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 108090000765 processed proteins & peptides Proteins 0.000 description 4
- 229960005202 streptokinase Drugs 0.000 description 4
- 102000005600 Cathepsins Human genes 0.000 description 3
- 108010084457 Cathepsins Proteins 0.000 description 3
- YMWUJEATGCHHMB-UHFFFAOYSA-N Dichloromethane Chemical compound ClCCl YMWUJEATGCHHMB-UHFFFAOYSA-N 0.000 description 3
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 230000004913 activation Effects 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 238000001704 evaporation Methods 0.000 description 3
- 230000008020 evaporation Effects 0.000 description 3
- 230000036541 health Effects 0.000 description 3
- 210000004072 lung Anatomy 0.000 description 3
- FEMOMIGRRWSMCU-UHFFFAOYSA-N ninhydrin Chemical compound C1=CC=C2C(=O)C(O)(O)C(=O)C2=C1 FEMOMIGRRWSMCU-UHFFFAOYSA-N 0.000 description 3
- 238000011533 pre-incubation Methods 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 239000000741 silica gel Substances 0.000 description 3
- 229910002027 silica gel Inorganic materials 0.000 description 3
- WEQJQNWXCSUVMA-NEPJUHHUSA-N (2s)-1-[(2r)-2-azaniumyl-3-phenylpropanoyl]pyrrolidine-2-carboxylate Chemical compound C([C@@H](N)C(=O)N1[C@@H](CCC1)C(O)=O)C1=CC=CC=C1 WEQJQNWXCSUVMA-NEPJUHHUSA-N 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 108010014173 Factor X Proteins 0.000 description 2
- 102000009123 Fibrin Human genes 0.000 description 2
- 108010073385 Fibrin Proteins 0.000 description 2
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 2
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- FXHOOIRPVKKKFG-UHFFFAOYSA-N N,N-Dimethylacetamide Chemical compound CN(C)C(C)=O FXHOOIRPVKKKFG-UHFFFAOYSA-N 0.000 description 2
- 108010094028 Prothrombin Proteins 0.000 description 2
- 102100027378 Prothrombin Human genes 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 230000002159 abnormal effect Effects 0.000 description 2
- 238000009825 accumulation Methods 0.000 description 2
- WJGAPUXHSQQWQF-UHFFFAOYSA-N acetic acid;hydrochloride Chemical compound Cl.CC(O)=O WJGAPUXHSQQWQF-UHFFFAOYSA-N 0.000 description 2
- 239000003146 anticoagulant agent Substances 0.000 description 2
- 229940127219 anticoagulant drug Drugs 0.000 description 2
- 239000000987 azo dye Substances 0.000 description 2
- 239000003480 eluent Substances 0.000 description 2
- 229950003499 fibrin Drugs 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 150000002431 hydrogen Chemical class 0.000 description 2
- 230000000951 immunodiffusion Effects 0.000 description 2
- 238000000691 measurement method Methods 0.000 description 2
- 108010088904 phenylalanylproline Proteins 0.000 description 2
- 125000006239 protecting group Chemical group 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 229940039716 prothrombin Drugs 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 238000002798 spectrophotometry method Methods 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- PGOHTUIFYSHAQG-LJSDBVFPSA-N (2S)-6-amino-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-1-[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-4-methylsulfanylbutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-5-carbamimidamidopentanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-3-hydroxypropanoyl]amino]-4-methylpentanoyl]amino]-3-sulfanylpropanoyl]amino]-4-methylsulfanylbutanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-hydroxybutanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-4-methylpentanoyl]amino]-3-hydroxybutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-oxopentanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]-3-carboxypropanoyl]amino]-3-hydroxypropanoyl]amino]-5-oxopentanoyl]amino]-5-oxopentanoyl]amino]-3-phenylpropanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-4-oxobutanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-carboxybutanoyl]amino]-5-oxopentanoyl]amino]hexanoic acid Chemical compound CSCC[C@H](N)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)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)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1cnc[nH]1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(O)=O PGOHTUIFYSHAQG-LJSDBVFPSA-N 0.000 description 1
- RRONHWAVOYADJL-OAHLLOKOSA-N (2r)-3-phenyl-2-(phenylmethoxycarbonylamino)propanoic acid Chemical compound C([C@H](C(=O)O)NC(=O)OCC=1C=CC=CC=1)C1=CC=CC=C1 RRONHWAVOYADJL-OAHLLOKOSA-N 0.000 description 1
- JXGVXCZADZNAMJ-NSHDSACASA-N (2s)-1-phenylmethoxycarbonylpyrrolidine-2-carboxylic acid Chemical compound OC(=O)[C@@H]1CCCN1C(=O)OCC1=CC=CC=C1 JXGVXCZADZNAMJ-NSHDSACASA-N 0.000 description 1
- IEQAICDLOKRSRL-UHFFFAOYSA-N 2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-(2-dodecoxyethoxy)ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethanol Chemical compound CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO IEQAICDLOKRSRL-UHFFFAOYSA-N 0.000 description 1
- VFRCXEHNAFUTQC-UHFFFAOYSA-N 2-[[2-(phenylmethoxycarbonylamino)acetyl]amino]acetic acid Chemical compound OC(=O)CNC(=O)CNC(=O)OCC1=CC=CC=C1 VFRCXEHNAFUTQC-UHFFFAOYSA-N 0.000 description 1
- TYMLOMAKGOJONV-UHFFFAOYSA-N 4-nitroaniline Chemical compound NC1=CC=C([N+]([O-])=O)C=C1 TYMLOMAKGOJONV-UHFFFAOYSA-N 0.000 description 1
- 102000004411 Antithrombin III Human genes 0.000 description 1
- 108090000935 Antithrombin III Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- FERIUCNNQQJTOY-UHFFFAOYSA-N Butyric acid Natural products CCCC(O)=O FERIUCNNQQJTOY-UHFFFAOYSA-N 0.000 description 1
- 206010053567 Coagulopathies Diseases 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 108010000499 Thromboplastin Proteins 0.000 description 1
- 102000002262 Thromboplastin Human genes 0.000 description 1
- 229960005348 antithrombin iii Drugs 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000003851 biochemical process Effects 0.000 description 1
- 238000005842 biochemical reaction Methods 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 108010051381 carbobenzoxyglycylglycine Proteins 0.000 description 1
- 108010034591 carbobenzoxyphenylalanylglycine Proteins 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-N carbonic acid Chemical class OC(O)=O BVKZGUZCCUSVTD-UHFFFAOYSA-N 0.000 description 1
- 230000000963 caseinolytic effect Effects 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 230000035602 clotting Effects 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000012954 diazonium Substances 0.000 description 1
- 150000001989 diazonium salts Chemical class 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 230000020764 fibrinolysis Effects 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- VANNPISTIUFMLH-UHFFFAOYSA-N glutaric anhydride Chemical compound O=C1CCCC(=O)O1 VANNPISTIUFMLH-UHFFFAOYSA-N 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- ZFGMDIBRIDKWMY-PASTXAENSA-N heparin Chemical compound CC(O)=N[C@@H]1[C@@H](O)[C@H](O)[C@@H](COS(O)(=O)=O)O[C@@H]1O[C@@H]1[C@@H](C(O)=O)O[C@@H](O[C@H]2[C@@H]([C@@H](OS(O)(=O)=O)[C@@H](O[C@@H]3[C@@H](OC(O)[C@H](OS(O)(=O)=O)[C@H]3O)C(O)=O)O[C@@H]2O)CS(O)(=O)=O)[C@H](O)[C@H]1O ZFGMDIBRIDKWMY-PASTXAENSA-N 0.000 description 1
- 238000005984 hydrogenation reaction Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 229910001410 inorganic ion Inorganic materials 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000014508 negative regulation of coagulation Effects 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 239000013610 patient sample Substances 0.000 description 1
- 239000002806 plasmin inhibitor Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000010926 purge Methods 0.000 description 1
- 238000007430 reference method Methods 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000011896 sensitive detection Methods 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- 238000007711 solidification Methods 0.000 description 1
- 230000008023 solidification Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- YLQBMQCUIZJEEH-UHFFFAOYSA-N tetrahydrofuran Natural products C=1C=COC=1 YLQBMQCUIZJEEH-UHFFFAOYSA-N 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
- 229940033663 thimerosal Drugs 0.000 description 1
- 229960003766 thrombin (human) Drugs 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- HRXKRNGNAMMEHJ-UHFFFAOYSA-K trisodium citrate Chemical compound [Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O HRXKRNGNAMMEHJ-UHFFFAOYSA-K 0.000 description 1
- 229940038773 trisodium citrate Drugs 0.000 description 1
- PAFMAHIOSMYVGN-UHFFFAOYSA-N trisodium trinitrate Chemical compound [Na+].[Na+].[Na+].[O-][N+]([O-])=O.[O-][N+]([O-])=O.[O-][N+]([O-])=O PAFMAHIOSMYVGN-UHFFFAOYSA-N 0.000 description 1
- 238000001665 trituration Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0821—Tripeptides with the first amino acid being heterocyclic, e.g. His, Pro, Trp
- C07K5/0823—Tripeptides with the first amino acid being heterocyclic, e.g. His, Pro, Trp and Pro-amino acid; Derivatives thereof
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0802—Tripeptides with the first amino acid being neutral
- C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0802—Tripeptides with the first amino acid being neutral
- C07K5/0812—Tripeptides with the first amino acid being neutral and aromatic or cycloaliphatic
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0819—Tripeptides with the first amino acid being acidic
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/10—Tetrapeptides
- C07K5/1002—Tetrapeptides with the first amino acid being neutral
- C07K5/1005—Tetrapeptides with the first amino acid being neutral and aliphatic
- C07K5/1013—Tetrapeptides with the first amino acid being neutral and aliphatic the side chain containing O or S as heteroatoms, e.g. Cys, Ser
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
- C12Q1/37—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase involving peptidase or proteinase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/56—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving blood clotting factors, e.g. involving thrombin, thromboplastin, fibrinogen
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q2337/00—N-linked chromogens for determinations of peptidases and proteinases
- C12Q2337/10—Anilides
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q2337/00—N-linked chromogens for determinations of peptidases and proteinases
- C12Q2337/30—Naphthyl amides, e.g. beta-NA, 2-NA, 4-methoxy-beta-naphthylamine, i.e. 4MNA
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
- G01N2333/968—Plasmin, i.e. fibrinolysin
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
- G01N2333/974—Thrombin
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2400/00—Assays, e.g. immunoassays or enzyme assays, involving carbohydrates
- G01N2400/10—Polysaccharides, i.e. having more than five saccharide radicals attached to each other by glycosidic linkages; Derivatives thereof, e.g. ethers, esters
- G01N2400/38—Heteroglycans, i.e. polysaccharides having more than one sugar residue in the main chain in either alternating or less regular sequence, e.g. gluco- or galactomannans, e.g. Konjac gum, Locust bean gum, Guar gum
- G01N2400/40—Glycosaminoglycans, i.e. GAG or mucopolysaccharides, e.g. chondroitin sulfate, dermatan sulfate, hyaluronic acid, heparin, heparan sulfate, and related sulfated polysaccharides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/802—Chromogenic or luminescent peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/28—Bound to a nonpeptide drug, nonpeptide label, nonpeptide carrier, or a nonpeptide resin
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Engineering & Computer Science (AREA)
- Physics & Mathematics (AREA)
- Immunology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Analytical Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Hematology (AREA)
- Neurosurgery (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US05/930,826 US4275153A (en) | 1978-08-03 | 1978-08-03 | Analytical fluorogenic substrates for proteolytic enzymes |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NO792553L true NO792553L (no) | 1980-02-05 |
Family
ID=25459832
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO792553A NO792553L (no) | 1978-08-03 | 1979-08-02 | Analytiske fluorogene substrater for proteolytiske enzymer |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US4275153A (fr) |
| EP (1) | EP0016800B1 (fr) |
| JP (1) | JPS5729999B2 (fr) |
| CA (1) | CA1152494A (fr) |
| DE (1) | DE2967581D1 (fr) |
| IT (1) | IT1117757B (fr) |
| NO (1) | NO792553L (fr) |
| WO (1) | WO1980000351A1 (fr) |
Families Citing this family (34)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2936543A1 (de) * | 1979-09-10 | 1981-04-09 | Behringwerke Ag, 3550 Marburg | Chromogene verbindungen |
| CA1161432A (fr) * | 1980-02-12 | 1984-01-31 | Lars G. Svendsen | Derives de tripeptides et application pour le dosage des enzymes |
| ATE8130T1 (de) * | 1980-08-25 | 1984-07-15 | Kabivitrum Ab | Peptidsubstrate zum bestimmen der proteaseaktivitaet. |
| JPS5856695A (ja) * | 1981-09-28 | 1983-04-04 | Nitto Boseki Co Ltd | 新規なトロンビン測定用基質 |
| DE3268329D1 (en) * | 1981-11-02 | 1986-02-13 | Pentapharm Ag | Process for the quantitative determination of the blood clotting factor xii in human plasma |
| JPS5925699A (ja) * | 1982-08-03 | 1984-02-09 | Torii Yakuhin Kk | 酵素活性測定方法 |
| US4473639A (en) * | 1982-09-15 | 1984-09-25 | Miles Laboratories, Inc. | Reagent strip test for antithrombin-III |
| CS231228B1 (en) * | 1982-10-01 | 1984-10-15 | Evzen Kasafirek | Biologically effective tri and tetrapeptide alkylamide derivatives and their processing method |
| DE3244030A1 (de) * | 1982-11-27 | 1984-05-30 | Behringwerke Ag, 3550 Marburg | Chromogene verbindungen, verfahren zu ihrer herstellung und ihre verwendung |
| US4621135A (en) * | 1983-12-08 | 1986-11-04 | Yeda Research & Development Company, Ltd. | Novel THF compositions |
| US4694070A (en) * | 1985-05-28 | 1987-09-15 | Coulter Electronics, Inc. | Water soluble xanthylium derivatives substrates |
| US4801534A (en) * | 1985-05-28 | 1989-01-31 | Coulter Electronics, Inc. | Water soluble zanthylium derivative substrates |
| SE461494B (sv) * | 1986-03-21 | 1990-02-19 | Thorsman & Co Ab | Faestanordning foer en elektrisk kopplingsdosa |
| EP0240914B1 (fr) * | 1986-04-01 | 1992-08-19 | Wako Pure Chemical Industries, Ltd. | Dérivés peptidiques et méthode de mesure de l'activité des substances physiologiquement actives utilisant ces substances comme substrats |
| US5023236A (en) * | 1988-04-07 | 1991-06-11 | Corvas, Inc. | Factor VII/VIIA active site inhibitors |
| US5593967A (en) * | 1990-08-31 | 1997-01-14 | Warner-Lambert Company | Cholecystokinin antagonists, their preparation and therapeutic use |
| US5391705A (en) * | 1991-03-15 | 1995-02-21 | Merrell Dow Pharmaceuticals Inc. | Polyfluorinated tripeptide thrombin inhibitors |
| US5534498A (en) * | 1992-01-30 | 1996-07-09 | Corvas International, Inc. | Trypsin inhibitors |
| US6759384B1 (en) | 1994-04-26 | 2004-07-06 | Aventis Pharmaceuticals Inc. | Factor Xa inhibitors |
| US5849510A (en) * | 1994-04-26 | 1998-12-15 | Selectide Corporation | Factor Xa inhibitors |
| RU2152954C1 (ru) * | 1994-04-26 | 2000-07-20 | Селектид Корпорейшн | Ингибиторы фактора ха |
| US5871946A (en) * | 1995-05-18 | 1999-02-16 | Coulter Corporation | Method for determining activity of enzymes in metabolically active whole cells |
| US5776720A (en) * | 1995-05-18 | 1998-07-07 | Coulter Corporation | Assay reagent |
| US5733719A (en) * | 1995-05-18 | 1998-03-31 | Coulter Corporation | Method of making an assay compound |
| US5698411A (en) * | 1995-05-18 | 1997-12-16 | Coulter Corporation | Method for determining activity of enzymes in metabolically active whole cells |
| US6069232A (en) * | 1995-10-02 | 2000-05-30 | Hoechst Marion Roussel, Inc. | Polyfluoroalkyl tryptophan tripeptide thrombin inhibitors |
| GB9525403D0 (en) * | 1995-12-13 | 1996-02-14 | Univ Sunderland | Method for monitoring enzymes |
| US5739354A (en) * | 1996-03-26 | 1998-04-14 | Hoechst Marion Roussel, Inc. | Process for the preparation of N-methyl-D-phenylalanyl-N- 1- 3- (aminoiminomethyl)amino!propyl!-3,3-difluoro-2-oxohexyl!-L-prolinamide |
| DE10116586B4 (de) * | 2001-04-03 | 2005-07-21 | Stief, Thomas, Dr.med. | Testsystem zur Bestimmung der Hämostaseaktivierung von biologischen Flüssigkeiten |
| WO2010087874A1 (fr) * | 2009-01-28 | 2010-08-05 | Anazyme, Llc | Compositions et méthodes pour le diagnostic des chocs |
| US8338127B2 (en) * | 2008-01-31 | 2012-12-25 | Anazyme | Testing a mammal for presence, progression or stage of a shock condition |
| WO2010059051A2 (fr) * | 2008-11-20 | 2010-05-27 | Nederlandse Organisatie Voor Toegepast-Natuurwetenschappelijk Onderzoek Tno | Diagnostic rapide de pathogènes basé sur fret |
| EP2189536A1 (fr) * | 2008-11-20 | 2010-05-26 | Nederlandse Organisatie voor toegepast-natuurwetenschappelijk Onderzoek TNO | Diagnostic rapide de l'anthrax par transfert de l'énergie de résonance par émission de fluorescence |
| JP2012517435A (ja) * | 2009-02-06 | 2012-08-02 | グリフオルス・セラピユーテイクス・インコーポレーテツド | プラスミン活性を決定するための組成物、キットおよび方法 |
Family Cites Families (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3862011A (en) * | 1971-08-16 | 1975-01-21 | Robert E Smith | Method for quantitatively determining enzyme concentrations in homogenates |
| SE380258B (sv) * | 1972-05-02 | 1975-11-03 | Bofors Ab | Nya diagnostiskt verksamma substrat med hog specificitet till trypsin och andra enzymer av typen peptidyl-peptid-hydrolaser |
| SE380257B (sv) * | 1972-05-02 | 1975-11-03 | Bofors Ab | Nya diagnostiskt verksamma substrat med hog specificitet till trombin och andra proteolytiska enzymer av typen peptidyl-peptid-hydrolaser |
| DE2527932C2 (de) * | 1974-07-02 | 1983-04-21 | Pentapharm AG, 4052 Basel | Säureadditionssalze von Tripeptidderivaten und deren Verwendung als Substrate zur Bestimmung von Plasmakallikrein |
| SE407058B (sv) * | 1974-12-05 | 1979-03-12 | Kabi Ab | Nya kromogena enzymsubstrat for serinproteaser |
| US4162941A (en) * | 1974-12-05 | 1979-07-31 | Ab Kabi | Method for determining a proteolytic enzyme |
| CH622286A5 (fr) * | 1975-06-23 | 1981-03-31 | Pentapharm Ag | |
| US4137225A (en) * | 1975-07-11 | 1979-01-30 | Ab Kabi | Novel chromogenic enzyme substrates |
| SE407571B (sv) * | 1975-07-11 | 1979-04-02 | Kabi Ab | Nya kromogena enzymsubstrat for serinproteaser |
| US4169015A (en) * | 1975-07-11 | 1979-09-25 | Ab Kabi | Novel chromogenic thrombin substrates |
| US4056519A (en) * | 1976-05-10 | 1977-11-01 | Eli Lilly And Company | Substrate for assay of plasmin |
| CH634662A5 (de) * | 1976-05-28 | 1983-02-15 | Pentapharm Ag | Verwendung von tripeptidderivaten zur quantitativen bestimmung von plasminogen-aktivatoren. |
| US4167449A (en) * | 1976-07-29 | 1979-09-11 | American Hospital Supply Corporation | Composition and method for determining transferase and protease activity |
| SE437153B (sv) * | 1976-12-01 | 1985-02-11 | Kabi Ab | Specifika kromogena enzymsubstrat for serinproteaser |
| US4215047A (en) * | 1977-06-06 | 1980-07-29 | Ajinomoto Company Incorporated | 7-(Arginylamino)-4-methylcoumarins |
| CA1087075A (fr) * | 1977-08-05 | 1980-10-07 | Robert J. Gargiulo | Produit et methode de dosage de l'activite de la transferase et de la protease |
| US4155916A (en) * | 1977-08-29 | 1979-05-22 | Dolbeare Frank A | Fluorescence method for enzyme analysis which couples aromatic amines with aromatic aldehydes |
| SE7801373L (sv) * | 1978-02-07 | 1979-08-08 | Kabi Ab | Lett spjelkbara substrat for kvantifiering av proteaser |
-
1978
- 1978-08-03 US US05/930,826 patent/US4275153A/en not_active Expired - Lifetime
-
1979
- 1979-06-15 DE DE7979900842T patent/DE2967581D1/de not_active Expired
- 1979-06-15 JP JP50117779A patent/JPS5729999B2/ja not_active Expired
- 1979-06-15 WO PCT/US1979/000421 patent/WO1980000351A1/fr unknown
- 1979-07-05 CA CA000331214A patent/CA1152494A/fr not_active Expired
- 1979-07-31 IT IT49905/79A patent/IT1117757B/it active
- 1979-08-02 NO NO792553A patent/NO792553L/no unknown
-
1980
- 1980-03-11 EP EP79900842A patent/EP0016800B1/fr not_active Expired
Also Published As
| Publication number | Publication date |
|---|---|
| IT1117757B (it) | 1986-02-24 |
| JPS5729999B2 (fr) | 1982-06-25 |
| DE2967581D1 (en) | 1986-04-10 |
| EP0016800A1 (fr) | 1980-10-15 |
| US4275153A (en) | 1981-06-23 |
| EP0016800A4 (fr) | 1981-01-08 |
| JPS55500538A (fr) | 1980-08-21 |
| WO1980000351A1 (fr) | 1980-03-06 |
| IT7949905A0 (it) | 1979-07-31 |
| EP0016800B1 (fr) | 1986-03-05 |
| CA1152494A (fr) | 1983-08-23 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| NO792553L (no) | Analytiske fluorogene substrater for proteolytiske enzymer | |
| US4336186A (en) | Analytical fluorogenic substrates for proteolytic enzymes | |
| US4784944A (en) | Prothrombin time determining reagent and methods of using and preparing the same | |
| DK149333B (da) | Tripeptidderivater samt salte deraf med mineralsyrer eller organiske syrer til anvendelse som substrater til kvantitativ bestemmelse af thrombin og thrombinlignende enzymer, ecarinthrombin, plasmin og plasminlignende enzymer samt proenzymer, proenzymaktivatorer og enzyminhibitorer herfor i legemsvaeskerfra mennesker og pattedyr samt i dyriske celleekstrakter | |
| Bergström et al. | Determination of vitamin K sensitive coagulation factors in plasma. Studies on three methods using synthetic chromogenic substrates | |
| EP0034586B1 (fr) | Derives de peptides de 4-trifluoromethylcoumarine et leurs utilisations dans les analyses de proteinase | |
| IE863167L (en) | Gram negative bacteria test | |
| Main et al. | The determination of human-serum-cholinesterase activity with o-nitrophenyl butyrate | |
| NO164201B (no) | Reagens for spektrofotometrisk bestemmelse av tilstedevaerelsen av leukocytter, esterase eller protease i en proeve, forsoeksinnretning omfattende denne og fremgangsmaate til bestemmelse av tilstedevaerelsen av de nevnte stoffene. | |
| Mitchell et al. | Fluorescent substrate assay for antithrombin III | |
| US5985582A (en) | Thrombin-based assay for antithrombin III | |
| US4167449A (en) | Composition and method for determining transferase and protease activity | |
| DK162179B (da) | Reagens til ettrinsbestemmelse af den aktiverede partielle thromboplastintid samt reagensets anvendelse | |
| NO151792B (no) | Fremgangsmaate ved bestemmelse av prothrombin i biologisk materiale og reagens for anvendelse ved fremgangsmaaten | |
| Tanaka et al. | A sensitive and specific assay for granulocyte elastase in inflammatory tissue fluid using L-pyroglutamyl-L-prolyl-L-valine-p-nitroanilide | |
| JPH0889293A (ja) | プロテインｃ／プロテインｓ系の障害を検出する方法 | |
| EP0360871B2 (fr) | Procede de mesure de l'activite biologique de l'antithrombine iii et trousse d'essai pour sa mesure | |
| EP0168738B1 (fr) | Essai à une étape pour inhibiteurs de protéinase | |
| Pochron et al. | A fluorescent substrate assay for plasminogen | |
| Ratnoff | Studies on the inhibition of ellagic acid-activated Hageman factor (factor XII) and Hageman factor fragments | |
| Vinazzer | Photometric assay of antithrombin III with a chromogenic substrate | |
| CA1276391C (fr) | Substrats de derive de xanthylium hydrosoluble | |
| US4801534A (en) | Water soluble zanthylium derivative substrates | |
| US4260681A (en) | Reagent system and method for assaying peptidase enzymes | |
| EP0318571B1 (fr) | Determination des constituants actifs dans une proteolyse |