Effect of polylysine on the activation of prothrombin. Polylysine substitutes for calcium ions and factor V in the factor Xa catalyzed activation of prothrombin
- 27 July 1976
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 15 (15) , 3265-3269
- https://doi.org/10.1021/bi00660a016
Abstract
Polylysine has been demonstrated to dramatically accelerate the rate of the factor Xa catalyzed activation of both prothrombin and prethrombin 1. Under these experimental conditions (pH 8.0, 23.degree. C), no detectable activation of prothrombin [bovine] or prethrombin 1 occurred with either factor Xa or polylysine alone. The activation of prethrombin 2, the direct precursor of .alpha.-thrombin, by factor Xa was not stimulated by polylysine. The activation of either prothrombin or prethrombin 1 by factor Xa in the presence of polylysine was partially inhibited by the presence of 5 mM CaCl2. Electrophoretic analysis in sodium dodecyl sulfate showed that the products that were formed in the above activation system comigrated with the reaction products derived from prothrombin activated by factor Xa in the presence of Ca ions and phospholipid. Polylysine apparently stimulated the factor Xa-catalyzed activation of prothrombin by replacing the combination of Ca ions and factor V.This publication has 5 references indexed in Scilit:
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