Benzyl p-guanidinothiobenzoate hydrochloride, a new active-site titrant for trypsin and trypsin-like enzymes
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چکیده
منابع مشابه
Benzyl p-guanidinothiobenzoate hydrochloride, a new active-site titrant for trypsin and trypsin-like enzymes.
Benzyl p-guanidinothiobenzoate hydrochloride was synthesized and demonstrated to be useful for active-site titration of bovine trypsin, bovine thrombin, human lung tryptase, bovine activated protein C, human Factor XIIa fragment and bovine Factor Xa beta. The titration is based on rapid formation of a stable acyl-enzyme with a stoichiometric release of benzyl thiol. Thiol production is measured...
متن کاملIntroduction of a cysteine protease active site into trypsin.
Active site serine 195 of rat anionic trypsin was replaced with a cysteine by site-specific mutagenesis in order to determine if a thiol group could function as the catalytic nucleophile in serine protease active site environment. Two genetically modified rat thiol trypsins were generated; the first variant contained a single substitution of Ser195 with Cys (trypsin S195C) while the second vari...
متن کاملThe Equilibrium between Active Native Trypsin and Inactive Denatured Trypsin
There is a mobile equilibrium between the native and denatured forms of trypsin which depends on the concentrations of acid, alkali, and alcohol and on the temperature. The heat of denaturation in 0.01 N hydrochloric acid calculated from the effect of temperature on the equilibrium constant is -67,600 calories per mole.
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The arginine amidase and arginine esterase activity of human plasma is compared with that of trypsin, thrombin, plasmin, and kallikrein by using the homologous synthetic amino acid substrates, benzoyl arginine amide (BAA) and benzoyl arginine ethyl ester (BAEE). Hydrolyses of BAA and BAEE in plasma are distinguished by several features: pH optimum, heat stability, storage stability, effect of d...
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The binding of thionine (3,6-diaminophenothiazine) to trypsin is associated with a red shift in the visible absorption spectrum of the dye. Spectrophotometric titration and equilibrium dialysis measurements are consistent with the presence of a single thionine-binding site on the trypsin molecule. At pH 7 and 4O, &is8 for the trypsin-thionine complex is 1.2 X lOUs M. The dye is displaced from t...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1983
ISSN: 0264-6021
DOI: 10.1042/bj2150287