Purification of Streptokinase and Human Plasmin and Their Interaction

W. F Blatt; H Segal; J. L Gray

doi:10.1055/s-0038-1654836

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1964; 11(02): 393-403
DOI: 10.1055/s-0038-1654836

Originalarbeiten — Original Articles — Travaux Originaux

Schattauer GmbH

Purification of Streptokinase and Human Plasmin and Their Interaction

W. F Blatt^*

¹Biochemistry Division, US Army Medical Research Laboratory, Ft. Knox, Ky

,

H Segal

¹Biochemistry Division, US Army Medical Research Laboratory, Ft. Knox, Ky

,

J. L Gray

¹Biochemistry Division, US Army Medical Research Laboratory, Ft. Knox, Ky

› Author Affiliations

Abstract

Summary

Procedures have been described for the purification of streptokinase and human plasmin, and molecular weights of 42,600 and 88,800 respectively have been determined. Equilibration of streptokinase with plasmin solutions produced an inhibition of caseinolytic activity and indicated a mole-mole interaction. This inhibitory activity was lost following acid treatment. When these data are considered with the previously reported findings using plasminstreptokinase mixtures as plasminogen activators, it would appear that plasmin and streptokinase react to form a complex which has the ability to convert both human and bovine plasminogen to plasmin.

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References

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