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Thromb Haemost 1964; 12(01): 126-136
DOI: 10.1055/s-0038-1655580
Originalarbeiten – Original Articles – Travaux Originaux
Schattauer GmbH

Fractionation of Plasminogen by Starch Gel Electrophoresis[*]

Karl H. Slotta
1   Departments of Biochemistry and Medicine, University of Miami School of Medicine, Miami, Florida
,
J. D Gonzalez
1   Departments of Biochemistry and Medicine, University of Miami School of Medicine, Miami, Florida
› Author Affiliations
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Publication Date:
27 June 2018 (online)

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Summary

When urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

* This investigations was supported by grant HE-04889-04 from the National Institutes of Health, Bethesda, Maryland.


 

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