Abstract
A significant amount of highly zymogenic chitin synthetase of Candida albicans was found to be associated with cytoplasmic particles (chitosomes). These cellular particles were isolated from metabolically activated C. albicans protoplasts after disruption by a mild method that minimizes vacuole rupture and consequent contamination of cellular fractions by vacuolar proteinases. Contamination of chitosomes by soluble cytosolic enzymes, vacuolar proteinases, vacuolar membranes, or other endomembranous structures was minimal, as indicated by the virtual absence of the following marker enzymes; α-glucosidase, carboxypeptidase Y, α-mannosidase, mannosyltransferase, and NADPH-cytochrome c reductase. Secretory enzymes such as acid phosphatase and other membrane-bound enzymes such as X-prolyl-dipeptidyl-aminopeptidase and leucine aminopeptidase did not sediment with the chitosomal chitin synthetase. These results support the idea that, in C. albicans as well as in other fungi, chitosomes are well-defined secretory organelles containing zymogenic chitin synthetase and not artifactual vesicles derived from plasma membrane and other membranous systems during cell breakage.
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