Biosynthesis of liver catalase in rats treated with allylisopropylacetylcarbamide. II. Double-labeling of catalase with (14C)leucine and delta-(3H)aminolevulinic acid.
Double-labeling of liver catalase [EC 1.11.1.6] with [14-c]leucine and delta-[3H]aminolevulinic 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.
D000622:Aminolevulinic Acid / Q000378:metabolism*; D000818:Animals; D002374:Catalase / Q000096:biosynthesis*; D007930:Leucine / Q000378:metabolism*; D007982:Levulinic Acids / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008830:Microbodies / Q000201:enzymology; D008862:Microsomes, Liver / Q000201:enzymology; D051381:Rats; D012270:Ribosomes / Q000201:enzymology; D014508:Urea / Q000031:analogs & derivatives* / Q000494:pharmacology; D014631:Valerates / Q000494:pharmacology
D007982:Levulinic Acids; D014631:Valerates; D000622:Aminolevulinic Acid; D014508:Urea; D002374:Catalase; D007930:Leucine; C005700:apronalide