Title

Regulation and solubilization of Candida albicans chitin synthetase

Authors

Phyllis C. Braun, Fairfield UniversityFollow
R. A. Calderone

Document Type

Article

Article Version

Publisher's PDF

Publication Date

1979

Abstract

A cytoplasmic component which inhibited the activation of chitin synthetase was studied in the dimorphic fungus Candida albicans. The inhibitor was found to be 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 molecular weight of the enzyme was estimated to be 400,000.

Comments

Copyright © 1979 American Society for Microbiology

The final publisher PDF has been archived here with permission from the copyright holder.

Publication Title

Journal of bacteriology

Repository Citation

Braun, Phyllis C. and Calderone, R. A., "Regulation and solubilization of Candida albicans chitin synthetase" (1979). Biology Faculty Publications. 69.
https://digitalcommons.fairfield.edu/biology-facultypubs/69

Published Citation

Braun, P. C., & Calderone, R. A. (1979). Regulation and solubilization of Candida albicans chitin synthetase. Journal of bacteriology, 140(2), 666-670.

Peer Reviewed