[Isolation and properties of the protein C activator from Agkistrodon halys halys venom].

Protein C activator from Agkistrodon halys halys venom has been purified by ion-exchange and gel-filtration chromatography. The purified enzyme consists of a single peptide chain with molecular weight of 34 kD. Its pH-optimum was the range of 7,5-8,0.

[Isolation and characteristics of the protein C activator from Agkistrodon halys halys snake venom].

Protein C activator from Agkistrodon halys halys venom has been isolated and purified by ion-exchange and gel-filtration chromatography. The purified enzyme consists of the single peptide-chain with molecular weight of 34 kDa. Its pH-optimum was in 7.

[Enzymes of snake venoms].

Snakes' venom is a mixture of biologically active substances, containing proteins and peptides. A number of these proteins interact with haemostasis system components. Activators and inhibitors affecting blood coagulation and fibrinolysis systems are of special interest.

[Purification and characterization of the fibrinolytic enzyme from Agkistrodon halys halys venom].

By Q-sepharose column ion-exchange chromatography, alkyl-sepharose column hydrophobic chromatography the purified fibrinogenolytic enzyme was obtained from Agkistrodon halys halys venom. It is a single peptide-chain with molecular weight about 28 kDa. It was founded that this enzyme cleaved A alpha-chain of fibrinogen, pH-optimum was determined in the range of 7.

[Aggregation of fibrinogen molecules in a solution].

Fibrinogen is found to be able to produce highly molecular aggregates in solution. Its maximal quantity aggregates at the temperature of 4 degrees C. The pH dependence of fibrinogen aggregates production is shown.