Microbody of n-alkane-grown yeast. Enzyme localization in the isolated microbody.
Microbodies appearing abundantly in n-alkane-grown cells of Candida tropicalis pK 233 were isolated by means of sucrose density gradient centrifugation. Electron microscopical observation showed that the microbodies isolated were intact. Localization of catalase and D-amino acid oxidase in the isolated microbodies was confirmed. Isocitrate lyase, melate synthase and NADP-linked isocitrate dehydrogenase were also located in the microbody, but malate dehydrogenase, citrate synthase, aconitase and NAD-linked isocitrate dehydrogenase were not. Neither cytochrome P-450 not NADPH-cytochrome c reductase, the components involved in the n-alkane hydroxylation system of the yeast, were detected in the microbody fraction.
D000473:Alkanes / Q000378:metabolism*; D002175:Candida / Q000201:enzymology* / Q000648:ultrastructure; D002374:Catalase / Q000032:analysis; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D006038:Glyoxylates / Q000378:metabolism; D008830:Microbodies / Q000201:enzymology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D009940:Organoids / Q000201:enzymology*
D000473:Alkanes; D006038:Glyoxylates; D002374:Catalase