Human heart citrate synthase: Purification, properties, kinetic and immunologic studies

Thomas C. Smitherman, Amal Mukherjee, Jack B. Robinson, Robert W. Butsch, E. Glen Richards, Paul A. Srere

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Abstract

Citrate synthase from human heart was purified by affinity chromatography with Sepharose-ATP. The molecular weight (100 000) and presence of two presumably identical subunits do not differ from other mammalian citrate synthases. However, the kinetic constants, and immunologic characteristics of the enzyme, differed from findings from other mammalian citrate synthases. The Km values for acetyl CoA (0.4 μm) and oxaloacetate (0.25 μm) were about an order of magnitude lower than that previously found for other mammalian (and eucaryotic) citrate synthases. The kinetic constants for the reverse reaction, Km for citrate (420 μm) and CoA (70 μm) were of similar magnitude to the values for other mammals. Anti-human heart antiserum developed a single precipitin line in an Ouchterlony plate against a heart extract, no precipitin line with brain, and a precipitin line with spurs against liver and kidney extract. Following myocardial infarction in men, the enzyme appeared in peripheral blood rarely and in low concentration in contrast with earlier experiences with experimental infarction in dogs.

Original languageEnglish
Pages (from-to)149-154,IN1-IN2,155-160
JournalJournal of Molecular and Cellular Cardiology
Volume11
Issue number2
DOIs
Publication statusPublished - Feb 1979

Keywords

  • Citrate synthase
  • Myocardial infarction

ASJC Scopus subject areas

  • Molecular Biology
  • Cardiology and Cardiovascular Medicine

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    Smitherman, T. C., Mukherjee, A., Robinson, J. B., Butsch, R. W., Glen Richards, E., & Srere, P. A. (1979). Human heart citrate synthase: Purification, properties, kinetic and immunologic studies. Journal of Molecular and Cellular Cardiology, 11(2), 149-154,IN1-IN2,155-160. https://doi.org/10.1016/0022-2828(79)90460-7