, Volume 37, Issue 1, pp 1–5 | Cite as

Pyruvate kinase-catalyzed ATP-formation in human red blood cell membranes

  • W. Schröter
  • W. Tillmann
  • G. Söndgen
Original Papers


Previous studies on the linkage between enzymatically catalyzed ATP-generating reactions in the red blood cell membrane and the sodium and potassium transport in the control of overall glycolysis of human erythrocytes were controversial. In this study a significant amount of pyruvate kinase activity is shown to be localized within the membrane. Membrane fragments produce 20.5μmol of ATP per 1010 membranes per hour from phosphoenolpyruvate and ADP. The kinetics of the membrane-localized pyruvate kinase do not differ from those of the enzyme from hemolysates. The results clearly document the presence of the second ATP-generating enzyme of glycolysis, pyruvate kinase, in human red blood cell membranes. The main fraction of the enzyme is deeply hidden in the lipid layers of the membrane. It can be demasked by mechanical desintegration of membranes at high levels of activity. It is suggested that the amount of the membrane-localized fraction of pyruvate kinase is related to the clinical severity of the hemolytic process in pyruvate kinase deficiency.

Key words

Pyruvate kinase deficiency Erythrocyte membrane 

Pyruvatkinase-katalysierte ATP-Bildung in der Erythrozytenmembran


Bisherige Untersuchungen über die Beziehungen zwischen enzymatisch-katalysierter ATP-Bildung in der Erythrozytenmembran und dem Natrium- und Kaliumtransport haben widersprüchliche Ergebnisse gezeigt. Die vorliegende Arbeit zeigt, daß die Membran menschlicher Erythrozyten eine nicht unbedeutende Menge Pyruvatkinase enthält. Membranbruchstücke bilden aus Phosphoenolpyruvat und ADP 20,5μMol ATP pro 101-Membranen pro Stunde. Die Kinetik der in der Membran lokalisierten Pyruvat0 kinasereaktion unterscheidet sich nicht von der des cytoplasmatischen Enzyms. Die Ergebnisse beweisen, daß die Pyruvatkinase, das zweite ATP-bildende Enzym der Glykolyse, in den Membranen menschlicher Erythrozyten vorhanden ist. Die Membranfraktion des Enzyms ist zwischen den Lipiden der Membran verborgen. Sie kann durch mechanische Zerstörung der Membran demaskiert werden. Es wird vermutet, daß die Menge der in der Membran lokalisierten Pyruvatkinase in Beziehung zur Schwere des hämoyltischen Prozesses beim Pyruvatkinasemangel steht.


Pyruvatkinasemangel Erythrozytenmembran 


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Copyright information

© Springer-Verlag 1978

Authors and Affiliations

  • W. Schröter
    • 1
  • W. Tillmann
    • 1
  • G. Söndgen
    • 1
  1. 1.Kinderklinik und Poliklinik der Universität GöttingenGöttingenFederal Republic of Germany

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