Thromb Haemost 1975; 33(02): 341-353
DOI: 10.1055/s-0038-1647886
Original Article
Schattauer GmbH

The Significance of Malate Dehydrogenase Isoenzymes in Human Blood Platelets

W Schneider
1   Medizinische Universitätsklinik und Poliklinik. Homburg/Saar, and Medizinische Universitätsklinik, Cologne, Germany
,
R Gross
1   Medizinische Universitätsklinik und Poliklinik. Homburg/Saar, and Medizinische Universitätsklinik, Cologne, Germany
› Author Affiliations
Further Information

Publication History

Received 21 August 1974

Accepted 11 December 1974

Publication Date:
02 July 2018 (online)

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Summary

Two MDH isoenzymes were detected in the homogenate of normal human blood platelets. According to their properties the cationic isoenzyme is compartmentalized in the mitochondria, the anionic one belongs to the cytoplasma. In spite of the few mitochondria in human blood platelets the proportion of the cationic enzyme is relatively high.

Both of these enzymes could belong to a transfer system for malate transport across the mitochondrial membrane. As human blood platelets do not contain creatine phosphate a system like that could be of significance for platelet function.