Regulation and solubilization of Candida albicans chitin synthetase

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Abstract
A cytoplasmic component which inhibited the activation of chitin synthetase was studied in the dimorphic fungus C. albicans. The inhibitor was heat stable and trypsin sensitive and was only effective when incubated with a vacuolar protease, an activator of chitin synthetase, before the activation of chitin synthetase. In addition, the particulate chitin synthetase from the yeast form of C. albicans was solubilized by a sodium cholate-digitonin extraction and subsequently was purified approximately 30-fold by Sepharose column chromatography and Amicon XM 100 filtration. Activity of the soluble enzyme was increased by the addition of trypsin or phosphatidyl serine. The MW of the enzyme was estimated to be 400,000.