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*
1   Biochemistry Division, US Army Medical Research Laboratory, Ft. Knox, Ky
,
H Segal
1   Biochemistry Division, US Army Medical Research Laboratory, Ft. Knox, Ky
,
J. L Gray
1   Biochemistry Division, US Army Medical Research Laboratory, Ft. Knox, Ky
› Institutsangaben
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Publikationsdatum:
24. Juli 2018 (online)

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.

* Now at the US Army Research Institute of Environmental Medicine, Natick, Massachusetts.