pH-dependent denaturation of extracellular aspartic proteinases from Candida species

J Med Vet Mycol. Jul-Aug 1995;33(4):275-8.

Abstract

The yeasts Candida albicans. Candida tropicalis, and Candida parapsilosis secrete aspartic proteinases which may enhance virulence. Profiles of pH-dependent irreversible denaturation of such enzymes were determined at 37 degrees C. C. albicans proteinases from both serotypes A and B maintained 50% of their activity near pH 7.25. Proteinases from C. parapsilosis and C. tropicalis lost 50% of their activity at pH 6.75 and pH 6.15, respectively. This suggests that in the infected host only proteinases of C. albicans maintain a native state for any length of time.

Publication types

  • Comparative Study

MeSH terms

  • Aspartic Acid Endopeptidases / chemistry*
  • Aspartic Acid Endopeptidases / isolation & purification
  • Aspartic Acid Endopeptidases / metabolism
  • Candida / classification
  • Candida / enzymology*
  • Candida / pathogenicity
  • Candida albicans / enzymology
  • Candida albicans / pathogenicity
  • Chromatography, DEAE-Cellulose
  • Hydrogen-Ion Concentration
  • Kinetics
  • Protein Denaturation*
  • Serotyping
  • Species Specificity
  • Virulence

Substances

  • Aspartic Acid Endopeptidases