Cytochemical localization of NADH oxidase in Candida albicans.
The application of a recently published technique to localize reduced nicotinamide adenine dinucleotide oxidase activity is described in glutaraldehyde-fixed Candida albicans. The reaction product appears as a finely granular precipitate on the mitochondrial cristae and on the central vacuolar membrane, and, if present, on the vacuolar contents. Fixation should be kept to a minimum and prolonged incubation times up to 2 hr are necessary to show these reactive sites. The reaction appears to be strongly substrate-dependent and not affected by cyanide. Exposure of C. albicans cells to the antimycotic miconazole resulted in a strong increase in reduced nicotinamide, adenine dinucleotide and oxidase activity. The hypothesis is put forward that this enzyme, together with peroxidative and catalatic enzymes, may be implicated in the mechanism by which miconazole exerts its lethal effect on C. albicans.
D002176:Candida albicans / Q000187:drug effects / Q000201:enzymology*; D006651:Histocytochemistry / Q000379:methods; D008825:Miconazole / Q000494:pharmacology; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis*
D008825:Miconazole; D009247:NADH, NADPH Oxidoreductases