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Studies on human heart citrate synthase

A Mukherjee, T C Smitherman, J B Robinson

    Advances in Myocardiology
    |January 1, 1980
    PubMed
    Summary
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    Human heart citrate synthase exhibits unique kinetic properties and immunological distinctiveness compared to other mammalian enzymes. This cardiac enzyme

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Citrate synthase is a key enzyme in the citric acid cycle, crucial for cellular energy production.
    • Mammalian citrate synthases share structural similarities but can exhibit functional variations.

    Purpose of the Study:

    • To purify and characterize citrate synthase from human heart.
    • To compare its kinetic and immunologic properties with other mammalian citrate synthases.

    Main Methods:

    • Purification of human heart citrate synthase using affinity chromatography with Sepharose-ATP.
    • Determination of molecular weight and subunit composition.
    • Kinetic analysis of substrate and product binding.
    • Immunological characterization using Ouchterlony double diffusion assays.

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    Main Results:

    • Human heart citrate synthase has a molecular weight of 100,000 with two identical subunits, consistent with other mammalian forms.
    • The enzyme displayed significantly lower Km values for acetyl-CoA (0.4 microM) and oxaloacetate (0.25 microM) compared to other mammalian citrate synthases.
    • Immunological studies showed specific reactivity with human heart extract and cross-reactivity with liver and kidney extracts, but not brain.
    • The enzyme was rarely detected in peripheral blood following myocardial infarction in humans.

    Conclusions:

    • Human heart citrate synthase possesses distinct kinetic parameters, suggesting specialized function.
    • The enzyme shows tissue-specific immunological characteristics.
    • Its low incidence in peripheral blood post-myocardial infarction contrasts with findings in canine models.