Enzyme cytochemistry of Candida albicans.
The application of a new preparation method for demonstrating the activities of hydrolytic and oxidative enzymes in Candida albicans is reported. The problem of inadequate penetration of fixatives into yeast cells has been solved by sectioning solidified pellets of the cells in the presence of glutaraldehyde, a procedure that yields a fairly well preserved ultrastructure and sufficient enzyme activities. The subcellular distribution of most specific and nonspecific phosphatases and of peroxidases is at variance with that found in mammalian cells. The activities toward beta-glycerophosphate, p-nitrophenylphosphate, adenosine triphosphate, adenosine monophosphate, thiamine pyrophosphate and glucose 6-phosphate are almost exclusively confined to the central vacuolar apparatus. Oxidative and peroxidative activities are demonstrated only in mitochondria. Specific marker enzymes for endoplasmic reticulum, plasmalemma, Golgi apparatus and peroxisomes in C. albicans are not found. The possible function of the various subcellular organelles in relation to their enzymatic content is discussed.
D000135:Acid Phosphatase / Q000032:analysis; D000469:Alkaline Phosphatase / Q000032:analysis; D002176:Candida albicans / Q000201:enzymology* / Q000648:ultrastructure; D002374:Catalase / Q000032:analysis*; D002467:Cell Nucleus / Q000201:enzymology; D003576:Electron Transport Complex IV / Q000032:analysis*; D006651:Histocytochemistry; D008854:Microscopy, Electron; D008928:Mitochondria / Q000201:enzymology; D010544:Peroxidases / Q000032:analysis*; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis*; D013347:Subcellular Fractions / Q000201:enzymology / Q000648:ultrastructure
D010544:Peroxidases; D002374:Catalase; D003576:Electron Transport Complex IV; D000469:Alkaline Phosphatase; D000135:Acid Phosphatase; D010744:Phosphoric Monoester Hydrolases