[Mechanism of a decrease of inducibility of tyrosine aminotransferase by carcinogenic aminoazo dyes. Absence of direct influence of o-aminoazotoluene on the enzyme molecules].
The effect of o-aminoazotoluene (OAT) on the activity of tyrosine aminotransferase (TAT) from mouse liver cytosol under its incubation in the presence of the systems providing for the metabolic activation of the cancerogen (liver microsomes and NADPH2) and dephosphorylation of TAT molecules (light mitochondria and ATP) was studied. It was shown that OAT has neither direct nor indirect (via the phsophorylation--dephosphorylation systems) effect on the activity of TAT. It was concluded that the decrease of TAT induction by hydrocortisone in vivo resulting from injection of OAT to the mice is not due to the direct influence of the cancerogen on the enzyme molecules.
D000818:Animals; D001391:Azo Compounds / Q000494:pharmacology*; D003600:Cytosol / Q000201:enzymology; D004790:Enzyme Induction / Q000187:drug effects; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D051379:Mice; D008862:Microsomes, Liver / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology; D014444:Tyrosine Transaminase / Q000096:biosynthesis*; D009762:o-Aminoazotoluene / Q000494:pharmacology*
D001391:Azo Compounds; D014444:Tyrosine Transaminase; D009762:o-Aminoazotoluene
K voprosu o mekhanizme snizheniia indutsibel'nosti tirozinaminotransferazy kantserogennymi aminoazokrasiteliami. Otsutstvie priamogo vliianĭia o-aminoazotoluola na ferment.