Correlation of H2O2 production and liver catalase during riboflavin deficiency and repletion in mammals.
A substantial decrease in liver peroxisomal catalase was found during riboflavin deficiency in rats. This decrease is greater than that found among other hemoproteins and seems to follow decrease in flavin-dependent peroxisomal oxidases. This is not due to a general depression of peroxisomal enzymes, since Cu-dependent urate oxidase activity was not changed. Furthermore, the level of catalase activity as well as flavin-dependent oxidases was restored by riboflavin repletion. These results suggest that hydrogen peroxide, the substrate for catalase produced by several flavoprotein oxidases, induces catalase in mammals as has been indicated for certain bacteria.
D000818:Animals; D002374:Catalase / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000096:biosynthesis*; D008099:Liver / Q000201:enzymology*; D008297:Male; D008830:Microbodies / Q000201:enzymology; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D051381:Rats; D011919:Rats, Inbred Strains; D012257:Riboflavin Deficiency / Q000201:enzymology / Q000378:metabolism*; D014503:Urate Oxidase / Q000302:isolation & purification
D006861:Hydrogen Peroxide; D002374:Catalase; D014503:Urate Oxidase