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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.

 

  • References

  • 1 Bergmeler H. U. Methoden der enzymatischen Analyse. Verlag Chemie GmbH, Weinheim/Bergstraße 1962
    Google Scholar
  • 2 Blonde D. J, Kresack E. J, Kosicki G. W. The effects of ions and freeze- thawing on supernatant and mitochondrial malate dehydrogenase. Canadian Journal of Biochemistry 1967; 45: 641
    PubMedGoogle Scholar
  • 3 Chappel J. B. In: Goodwin T. W, Lindberg O. (eds.) Biological Structure and Function Academic Press; London: 71 1961
  • 4 Chernyak N. B. Processes of formation and utilization of energy in human blood platelets. Clínica Chimica Acta 1965; 12: 244
    PubMedGoogle Scholar
  • 5 Colombo J. P, Richterich P, Possi E. Serum-Kreatinin-Phosphokinase: Bestimmung und diagnostische Bedeutung. Klinische Wochenschrift 1962; 40: 37
    CrossrefPubMedGoogle Scholar
  • 6 van Dam K, Meyer A. J. Oxidation and energy conservation by mitochondria. Annual Review of Biochemistry 1971; 40: 115
    CrossrefPubMedGoogle Scholar
  • 7 Delbrück A, Schimassek H, Bartsch K, Bücher T. Enzym-Verteilungsmuster in einigen Organen und in experimentellen Tumoren der Patte und der Maus. Biochemische Zeitschrift 1959; 331: 273
    PubMedGoogle Scholar
  • 8 Doery J. C. G, Hirsh J, Cooper I. Energy metabolism in human platelets. Interrelationship between glycolysis and oxidative metabolism. Blood 1970; 36: 159
    PubMedGoogle Scholar
  • 9 Doery J. C. G, Hirsh Jde Gruchy. Platelet glycolytic enzymes: effect of cellular disruption procedures on activity. British Journal of Haematology 1970; 19: 145
    CrossrefPubMedGoogle Scholar
  • 10 Englard SBreiger. Beef heart malic dehydrogenase. II. Preparation and properties of crystalline supernatant malic dehydrogenase.. Biochimica et Biophysica Acta 1962; 56: 571
    CrossrefPubMedGoogle Scholar
  • 11 Garland P. B, Randle P. J. Control of pyruvate dehydrogenase in the perfused rat heart by the intracellular concentration of acetylcoenzyme A. Biochemical Journal 1964; 91: 6C
    PubMedGoogle Scholar
  • 12 Gross R. In: Johnson S. A, Monto B. W, Rebuck J. W, Horn R. C. (eds.) Blood Platelets. Little, Brown and Co.; Boston: 407 1964
    Google Scholar
  • 13 Gross R, Löhr G. W, Waller H. D. Genetic defects in platelet metabolism as a cause of thrombocytopathias. In: Kowalski E, Niewiarowski S. (eds.) Biochemistry of Blood Platelets Academic Press; London and New York: 1967: 161
    Google Scholar
  • 14 Gross R, Schneider W. Neuere Untersuchungen über den Stoffwechsel der Thrombozyten. In: Deutsch E, Gerlach E, Moser K. (eds.) Metabolism and Membrane Permeability of Erythrocytes and Thrombocytes Thieme; Stuttgart: 1968: 206
    Google Scholar
  • 15 Gross R, Schneider W. Energy metabolism. In: Johnson S. A. (ed.) The Circulating Platelet Academic Press; New York and London: 1971: 123
    Google Scholar
  • 16 Hathaway J. A, Atkinson D. E. Kinetics of regulatory enzymes: effect of adenosine triphosphate on yeast citrate synthase. Biochemical and Biophysical Research Communications 1965; 20: 661
    CrossrefPubMedGoogle Scholar
  • 17 Karpatkin S, Charmatz A, Langer R. M. Incorporation of glucose, pyruvate, and citrate into platelet glycogen; glycogen synthetase and fructose-1,6-diphosphatase activity. Journal of Clinical Investigation 1970; 49: 140
    CrossrefPubMedGoogle Scholar
  • 18 Kitto B, Kaplan N. O. Purification and properties of chicken heart mitochondrial and supernatant malic dehydrogenases. Biochemistry 1966; 5: 3966
    CrossrefPubMedGoogle Scholar
  • 19 Kitto G. B, Lewis R. G. Purification and properties of tuna supernatant and mitochondrial malate dehydrogenases. Biochimica et Biophysica Acta 1967; 139: 1
    CrossrefPubMedGoogle Scholar
  • 20 Krebs H. A, Speake R. N, Hems R. Acceleration of renal gluconeogenesis by ketone bodies and fatty acids. Biochemical Journal 1965; 94: 712
    CrossrefPubMedGoogle Scholar
  • 21 Kun E, Volfin P. Tissue specifity of malate dehydrogenase isoenzymes. Kinetic discrimination by oxaloacetate and its mono- and difluoro analogues. Biochemical and Biophysical Research Communications 1966; 22: 187
    CrossrefPubMedGoogle Scholar
  • 22 Lowry O. H, Rosebrough N. J, Farr A. L, Randall R. J. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 1951; 193: 265
    PubMedGoogle Scholar
  • 23 Löhr G. W, Waller H. D, Gross R. Beziehungen zwischen Plättchenstoffwechsel und Retraktion des Blutgerinnsels. Deutsche Medizinische Wochenschrift 86 1961; 897-946.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 24 Lüscher E. F. Retraction activity of the platelets: biochemical background and physiological significance. In: Johnson S. A, Monto R. W, Rebuck J. W, Horn R. C. (eds.) Blood Platelets Little, Brown and Co.; Boston: 445
    Google Scholar
  • 25 Marcus A. J, Zucker-Franklin D, Safter L. B, Ullman H. L. Studies on human platelet granules and membranes. Journal of Clinical Investigation 1966; 45: 14
    CrossrefPubMedGoogle Scholar
  • 26 Mürer E. H. Clot retraction and energy metabolism of platelets. Effect and mechanism of inhibitors. Biochimica et Biophysica Acta 1969; 172: 266
    CrossrefPubMedGoogle Scholar
  • 27 Neumeister E, Otto P, Schmidt E, Schmidt F. W. Quantitative Bestimmung der Isoenzyme der Malat-Dehydrogenase, Glutamat-Oxalacetat-Trans-aminase und Lactat-Dehydrogenase im Serum bei Leberkrankheiten. Die Medizinische Welt 1965; 27: 1479
    PubMedGoogle Scholar
  • 28 Pette D. Aktivitätsmuster und Organmuster von Enzymen des energieliefernden Stoffwechsels. In: Aebi H, Mattenheimer H, Schmidt F. W. (eds.) Praktische Enzymologie Huber; Bern: 15 1968
    Google Scholar
  • 29 Rapoport S. M. Medizinische Biochemie. Volk und Gesundheit; Berlin: 1962
    Google Scholar
  • 30 Reith A, Möhr J, Schmidt E, Schmidt F. W, Wildhirt E. Isoenzyme und Veränderungen der IsozymVerteilung von Malat- und Isozitrat-Dehydrogenase und Glutamat-Oxalacetat-Transaminase in der normalen und pathologisch veränderten tierischen und menschlichen Leber. Klinische Wochenschrift 1964; 42: 909
    CrossrefPubMedGoogle Scholar
  • 31 Rodman N. F, Mason R. G, Brinkhous K. M. Some pathogenetic mechanisms of white thrombus formation: agglutination and self-destruction of the platelet. Federation Proceedings 1963; 22: 1356
    PubMedGoogle Scholar
  • 32 Rodman N. F, Mason R. G, Painter J. C, Brinkhous K.M. Fibrinogen-its role in platelet agglutination and agglutinate stability. Laboratory Investigation 1966; 15: 641
    PubMedGoogle Scholar
  • 33 Schmitz H, Schleipen T, Gross R. Freie Nukleotide in normalen menschlichen Blutplättchen. Klinische Wochenschrift 1962; 40: 13
    CrossrefPubMedGoogle Scholar
  • 34 Schneider W, Doenecke C, Scheurlen P. G, Gross R. Hemmung der Thrombozytenfunktion durch Azetylsalizylsäure. Die Medizinische Welt 1971; 22: 1262
    PubMedGoogle Scholar
  • 35 Schneider W, Schumacher K, Thiede B, Gross R. Chromatographic isolation of the LDH-isoenzymes of human blood platelets and an investigation of their enzyme kinetics. Thrombosis et Diathesis Haemorrhagica 1968; 20: 301
    PubMedGoogle Scholar
  • 36 Scott R. B. Activation of glycogen Phosphorylase in blood platelets. Blood 1967; 30: 321
    PubMedGoogle Scholar
  • 37 Shrago E. Cytoplasmic characteristics of human erythrocyte malic dehydrogenase. Archives of Biochemistry and Biophysics 1965; 109: 57
    CrossrefPubMedGoogle Scholar
  • 38 Siegel L, Englard S. Beef heart malic dehydrogenases. I. Properties of the enzyme purified from extracts of acetone-dried powders.. Biochimica et Biophysica Acta 1961; 54: 67
    CrossrefPubMedGoogle Scholar
  • 39 Stetner M, Kuramoto A. Energy Metabolism of aggregating platelets. Series Haematologica 1971; IV: 98
    PubMedGoogle Scholar
  • 40 Thorne C. J. R. Characterization of two malic dehydrogenases from rat liver. Biochimica et Biophysica Acta 1960; 42: 175
    CrossrefPubMedGoogle Scholar
  • 41 Thorne C. J. R, Cooper P. M. Preparation of pig heart supernatant malate dehydrogenase. Biochimica et Biophysica Acta 1963; 81: 397
    PubMedGoogle Scholar
  • 42 Thorne C. J. R, Grossman L. I, Kaplan N. O. Starch-gel electrophoresis of malate dehydrogenase. Biochimica et Biophysica Acta 1963; 73: 193
    CrossrefPubMedGoogle Scholar
  • 43 Waller H. D, Löhr G. W, Grignani F, Gross R. Über den Energiestoffwechsel normaler menschlicher Blutplättchen. Thrombosis et Diathesis Haemorrhagica 1959; 3: 520
    PubMedGoogle Scholar