TRANSAMINATION OF L-CYSTEINE IN RAT-LIVER MITOCHONDRIA

  • 1 January 1977
    • journal article
    • research article
    • Vol. 9  (1) , 91-96
Abstract
Transamination of L-cysteine in rat liver was examined. Specific activity of the reaction in mitochondria was found higher than that in cytosol. The mitochondrial reaction was shown to be catalyzed by 2 different enzymes. The 1st was active with 2-oxoglutarate and inactivated by heating at 60.degree. C for 10 min; the activity was protected from heat activation by the presence of 2-oxoglutarate. The 2nd enzyme was active with pyruvate and more stable than the 1st under heat treatment; 2-oxoglutarate had little protective effect on this 2nd enzyme. The 2nd enzyme activities were separated by heat treatment and ammonium sulfate fractionation.

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