A New Method for Plasminogen Standardization
- 1 January 1968
- journal article
- schattauer gmbh
- Published by Georg Thieme Verlag KG in Thrombosis and Haemostasis
- Vol. 20 (03/04) , 548-554
- https://doi.org/10.1055/s-0038-1651297
Abstract
A method for the standardization of human plasminogen is proposed, based on the stoichiometric interaction between plasminogen and streptokinase, resulting in inhibition of proteolytic activity. Activation of a constant amount of plasminogen with increasing amounts of streptokinase yields linearly decreasing activities, as a function of streptokinase, with a sharp transition to a constant residual level. The point of transition corresponds to complete saturation of plasmin with streptokinase in a 1:1 molar ratio, and is therefore a measure of the amount of plasminogen present initially, in terms of streptokinase equivalents. The equivalence point is independent of the kind of protein substrate used, buffer, pH, length of digestion and, within limits, temperature. The method, therefore, is not subject to the variations commonly encountered in the usual determination based on specific activity measurements. * Supported by Grant 67- 866 from the American Heart Association and Grant ROI HE1 1442 from the National Institutes of Health. ** Present address: Rhode Island Hospital, Providence, Rhode Island 02903.Keywords
This publication has 1 reference indexed in Scilit:
- The effects of guanidine compounds on the activation of human plasminogen by streptokinase and on the rates of hydrolysis of p-toluenesulfonyl-L-arginine methyl ester by plasmin and ActivatorBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966