Properties of catalase purified from whole cells and peroxisomes of n-alkane-grown Candida tropicalis.
Peroxisomes appear profusely, in harmony with a marked enhancement of catalase activity level, in yeast cells growing on n-alkanes or higher fatty acids as the sole carbon source. Catalase (H2O2:H2O2 oxidoreductase, EC 1.11.1.6) was purified to homogeneity from the crude extract and from the peroxisome-containing particulate fraction of alkane-grown Candida tropicalis cells. The purified enzyme from each source was a similar protein of molecular weight 210000 composed of four identical subunits of molecular weight 54000, namely a kind of homotetramer. The enzyme contained one molecule of heme per subunit, giving the absorption spectrum characteristic of hemoprotein. Beta-(3,4-Dihydroxyphenyl)-L-alanine served as a substrate for the peroxidatic reaction by the enzyme. Ouchterlony double-diffusion analysis and immunochemical titration with rabbit antiserum against peroxisomal catalase of n-alkane-grown C. tropicalis have indicated that cytoplasmic catalase of the yeast is immunologically indistinguishable with peroxisomal catalase.
D000473:Alkanes / Q000378:metabolism*; D002175:Candida / Q000201:enzymology*; D002374:Catalase / Q000302:isolation & purification / Q000378:metabolism*; D007120:Immunochemistry; D008830:Microbodies / Q000201:enzymology*; D009940:Organoids / Q000201:enzymology*; D013379:Substrate Specificity
D000473:Alkanes; D002374:Catalase