Activation of human prothrombin by a procoagulant fraction from the venom of Echis carinatus. Identification of a high molecular weight intermediate with thrombin activity.

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منابع مشابه

Blood Coagulation Induced by Iranian Saw-Scaled Viper (Echis Carinatus) Venom: Identification, Purification and Characterization of a Prothrombin Activator

  Objective(s): Echis carinatus is one of the venomous snakes in Iran. The venom of Iranian Echis carinatus is a rich source of protein with various factors affecting the plasma protein and blood coagulation factor. Some of these proteins exhibit types of enzymatic activities. However, other items are proteins with no enzymatic activity.   Materials and Methods: In order to study the mechanism ...

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blood coagulation induced by iranian saw-scaled viper (echis carinatus) venom: identification, purification and characterization of a prothrombin activator

objective(s): echis carinatus is one of the venomous snakes in iran. the venom of iranian echis carinatus is a rich source of protein with various factors affecting the plasma protein and blood coagulation factor. some of these proteins exhibit types of enzymatic activities. however, other items are proteins with no enzymatic activity.   materials and methods: in order to study the mechanism an...

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Blood Coagulation Induced by Iranian Saw-Scaled Viper (Echis Carinatus) Venom: Identification, Purification and Characterization of a Prothrombin Activator

OBJECTIVE(S) Echis carinatus is one of the venomous snakes in Iran. The venom of Iranian Echis carinatus is a rich source of protein with various factors affecting the plasma protein and blood coagulation factor. Some of these proteins exhibit types of enzymatic activities. However, other items are proteins with no enzymatic activity. MATERIALS AND METHODS In order to study the mechanism and ...

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15 صفحه اول

Differentiation between proteolytic activation and autocatalytic conversion of human prothrombin. Activation of recombinant human prothrombin and recombinant D419N-prothrombin by snake venoms from Echis carinatus and Oxyuranus scutellatus.

Recombinant human prothrombin (r-prothrombin) and recombinant mutant prothrombin with active site Asp419 substituted by Asn (D419N-prothrombin) were expressed in recombinant CHO cells, isolated and purified from the fermentation supernatant. The r-Prothrombin and D419N-prothrombin were digested by both Echis carinatus venom and Oxyuranus scutellatus venom. Prior to, during and after activation,...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1975

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)41038-7