Active site of bovine factor Xa. Characterization using substituted benzamidines as competitive inhibitors and affinity-labeling reagents.
نویسندگان
چکیده
منابع مشابه
The role of endothelium in factor Xa regulation: the effect of plasma proteinase inhibitors and hirudin.
The role of endothelium in the inhibition of human factor Xa was studied in a plasma environment. Human factor Xa can bind to and function on bovine aortic endothelium in a manner similar to that of bovine factor Xa. Approximately 70% of the bound factor Xa is subject to inhibition by plasma proteinase inhibitors, and the remaining 30% is irreversibly bound as part of a 125 Kd membrane-associat...
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Water molecules in the active site of an enzyme occupy a complex, heterogeneous environment, and the thermodynamic properties of active-site water are functions of position. As a consequence, it is thought that an enzyme inhibitor can gain affinity by extending into a region occupied by unfavorable water or lose affinity by displacing water from a region where it was relatively stable. Recent a...
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p-Nitrophenyl-p’-guanidinobenzoate is a suitable substrate for the titration of purified bovine Factor X which has been activated by a coagulant protein from Russell’s viper venom. Reaction of Factor Xa with p-nitrophenyl-P’-guanidinobenzoate occurs at the site which is responsible for the clotting activity of Factor Xa. Activation of bovine Factor X by the Russell’s viper venom coagulant prote...
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 255 5 شماره
صفحات -
تاریخ انتشار 1980