Biosynthesis of liver catalase in rats treated with allylisopropylacetylcarbamide. II. Double-labeling of catalase with (14C)leucine and .DELTA.-(3H)aminolevulinic acid.:II. Double-labeling of Catalase with [<sup>14</sup>C] Leucine and δ-[<sup>3</sup>H] Aminolevulinic Acid

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  • KAWAMATA Fumiko
    Department of Biochemistry, School of Pharmaceutical Sciences, Showa University
  • SAKURAI Toshiharu
    Department of Biochemistry, School of Pharmaceutical Sciences, Showa University
  • HIGASHI Tokuhiko
    Department of Biochemistry, School of Pharmaceutical Sciences, Showa University

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Description

Double-labeling of liver catalase [EC 1. 11. 1. 6] with [14C] leucine and δ-[3H] arninolevulinic acid was carried out both in vivo and in vitro using rats treated with allylisopropylacetylcarbamide (Sedormid). These radioactive precursors were incorporated into catalase at a lower rate than in normal rats. In particular, the incorporation of 3H was remarkably inhibited. The results suggest that the administration of Sedormid can inhibit synthesis of the protein moiety of catalase, and possibly interfere with the binding of heme to the catalase protein.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 78 (5), 975-980, 1975

    The Japanese Biochemical Society

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