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The major exoglucanase from Candida albicans : A non‐glycosylated secretory monomer related to its counterpart from Saccharomyces cerevisiae
Author(s) -
LunaArias Juan P.,
Andaluz Encarnación,
Ridruejo Juan C.,
Olivero Isabel,
Larriba Germán
Publication year - 1991
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320070808
Subject(s) - candida albicans , biology , biochemistry , saccharomyces cerevisiae , glycosylation , corpus albicans , enzyme , gel electrophoresis , amino acid , polyacrylamide gel electrophoresis , peptide sequence , microbiology and biotechnology , yeast , gene
Abstract Exoglucanases secreted by two different strains from Candida albicans have been purified to homogeneity. The purified enzyme from each strain behaved as a non‐glycosylated monomer (molecular weight 38 000) that was identical in terms of sodium dodecyl sulphate/polyacrylamide gel electrophoresis comigratin, amino acid analysis and amino terminal sequence. The amino acid composition was similar to that of the major exoglucanase from Saccharomyces cerevisiae . In addition, these two enzymes displayed a 50% homology in the first 35 amino acids of the amino terminus. Antibodies against the deglycosylated exoglucanase (treated with Endo H) from S. cerevisiae were reactive with the exoglucanase from C. albicans and vice versa . Immunoblotting proved to be a semiquantitative method to detect C. albicans antigen in culture fluids. The exoglucanase from C. albicans appears to enter the secretory pathway without undergoing N‐glycosylation.