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Updated: Jul 29, 2026

Separation of Bioactive Small Molecules, Peptides from Natural Sources and Proteins from Microbes by Preparative Isoelectric Focusing (IEF) Method
Published on: June 14, 2020
Isolation and identification of a 92-kDa stress induced protein from Candida albicans
E T Burt1, C O'Connor, B Larsen
1Department of Biochemistry, Des Moines University-Osteopathic Medical Center, IA 50312, USA. Edward.Burt@dsmu.edu
Abstract:
It was previously shown that the presence of estrogen enhances survival of Candida albicans under heat and oxidative stresses. A 92-kDa protein is inducible by heat shock and estrogen in C. albicans. Previous studies have described this protein as hsp90 because of its molecular size and heat inducibility as seen on electrophoretic gels and Western blots. In this study, ion exchange, hydroxyapatite and size exclusion chromatography were used to isolate a 92-kDa-protein band. The N-terminal sequence of isolated protein blotted onto a PVDF membrane was determined to be V-Q-S-?-V-L-G-F-P-R. This sequence is homologous to the N-terminal sequence of the MET6 gene product, cobalamin-independent methionine synthase, from Saccharomyces cerevisiae. The results of this study suggest that a cobalamin-independent methionine synthase homolog is inducible by heat and estrogen in C. albicans. This study also suggests that Candida hsp90 is more likely to exist as an 82-kDa protein as predicted by a previously described cDNA and not as a 92-kDa protein as reported in the literature.
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