The major exoglucanase from Candida albicans: a non-glycosylated secretory monomer related to its counterpart from Saccharomyces cerevisiae.
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 comigration, 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.
Luna-Arias
J P
JP
Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, Badajoz, Spain.
Andaluz
E
E
Ridruejo
J C
JC
Olivero
I
I
Larriba
G
G
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000908:Antibodies, Fungal / Q000276:immunology; D015153:Blotting, Western; D002176:Candida albicans / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D043326:Glucan 1,3-beta-Glucosidase; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D001617:beta-Glucosidase / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification
D000596:Amino Acids; D000908:Antibodies, Fungal; D001617:beta-Glucosidase; D043326:Glucan 1,3-beta-Glucosidase