Thromb Haemost 1963; 10(01): 133-145
DOI: 10.1055/s-0038-1654769
Originalarbeiten — Original Article — Travaux Originaux
Schattauer GmbH

The Streptokinase Activation of Human Plasminogen. Direct Analysis of the Activation Mixture

Ubaldo Rifé*
1   Department of Biophysics, State University of New York at Buffalo School of Medicine, Buffalo, N. Y. (U. S. A.)
,
Sidney Shulman*
1   Department of Biophysics, State University of New York at Buffalo School of Medicine, Buffalo, N. Y. (U. S. A.)
› Author Affiliations
Further Information

Publication History

Publication Date:
22 June 2018 (online)

Summary

1. Incubated mixtures of plasminogen and streptokinase revealed three components in optical electrophoresis at pH 2.00. The fastest component was identified as plasmin, and the other two components were taken to represent plasminopeptides A and B, in accordance with their mobilities.

2. By means of gel filtration, it was possible to show the presence of three constituents. The major one had caseinolytic activity, while the other two had no such activity.

3. From the known properties of molecular exclusion by various Sephadex preparations, it was estimated that the two peptides had molecular weights of approximately 10,000.

4. The possibility of improving the purity of plasmin preparations was demonstrated.

* Present address: Universidad Nacional de Cordoba, Instituto de Biología Celular, Cordoba, Argentina.


** Recipient of a Research Career Development Award (GM-K3-1377) from the U. S Public Health Service.


 
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