Enzymatic Studies on the Metabolism of the Tetrahydrofurfuryl Mercaptan Moiety of Thiamine Tetrahydrofurfuryl Disulfide:IV. Induction of Microsomal S-Transmethylase, and Sulfide and Sulfoxide Oxygenases in the Drug-treated Rat

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  • FUJITA Takeshi
    Biological Research Laboratories, Central Research Division, Takeda Chem. Ind., Ltd.
  • TERAOKA Akio
    Biological Research Laboratories, Central Research Division, Takeda Chem. Ind., Ltd.
  • SUZUOKI Ziro
    Biological Research Laboratories, Central Research Division, Takeda Chem. Ind., Ltd.

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Description

The influence of drug pretreatment was investigated on three novel microsomal enzyme activities: S-transmethylase, and sulfide and sulfoxide oxygenases, responsible for the biotransformation of foreign mercaptan sulfur in the rat. S-Transmethylase activity was induced by treatment with 3-methylcholanthrene, but not by phenobarbital. On the other hand, both oxygenase activities were enhanced about 2-fold by treatment with phenobarbital, but not by 3-methylcholanthrene administration.<br> These three enzyme activities were not appreciably influenced by treatment with tetrahydrofurfuryl mercaptan, methyl tetrahydrofurfuryl sulfide and its sulfoxide, which were the respective substrates. Thiamine tetrahydrofurfuryl disulfide, the parent compound of these metabolites, failed to induce these three enzyme activities when administered either intraperitoneally or orally to the rat. Pretreatment with thiamine tetrahydrofurfuryl disulfide and related metabolites caused no significant influence on either the microsomal activities of aniline hydroxylase [EC 1. 14. 1. 1], aminopyrine N-demethylase, and NADPH-cytochrome c reductase, or the microsomal content of cytochrome P-450.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 74 (4), 739-745, 1973

    The Japanese Biochemical Society

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