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Study of the Clotting, Esterase and Platelet Aggregating Activities of Thrombin, Acetylated Thrombin and Reptilase®
Author(s) -
TANGEN O.,
BYGDEMAN S.
Publication year - 1972
Publication title -
scandinavian journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0036-553X
DOI - 10.1111/j.1600-0609.1972.tb00949.x
Subject(s) - thrombin , chemistry , platelet , fibrinogen , esterase , biochemistry , acetylation , thrombin time , enzyme , biology , immunology , partial thromboplastin time , gene
The ability of thrombin, acetylated thrombin and Reptilaser̀ to aggregate suspensions of gel filtered human and rabbit platelets in a protein free medium has been investigated. Thrombin had a pronounced aggregating effect in contrast to acetylated thrombin and Reptilaser̀ which did not aggregate platelets from any of two species and in any concentrations tested. These results indicate that the esterase activity of thrombin, which is retained in the acetylated enzyme, is not related to the platelet aggregating capacity of thrombin. The proteolytic activity of thrombin is a more likely candidate for the role of platelet aggregation. However, the particular proteolytic activity resulting in the hydrolysis of fibrinopeptide A from fibrinogen does not seem to be involved, as Reptilaser̀ has no platelet aggregating effect.