Comparison of secretory acid proteinases from Candida tropicalis, C. parapsilosis and C. albicans

Microbiol Immunol. 1992;36(10):1099-104. doi: 10.1111/j.1348-0421.1992.tb02113.x.

Abstract

Acid proteinases secreted by Candida tropicalis and C. parapsilosis were newly isolated. Their physico-chemical and enzymatic properties of molecular weight, pH stability, isoelectric points, specific activity, and N-terminal amino acid sequences were determined and compared with those of a C. albicans acid proteinase. The two acid proteinases secreted by C. parapsilosis were found to be new enzymes in their molecular weights. The acid proteinases from C. tropicalis and C. parapsilosis showed lower activity at neutral pH, less resistance to neutral and alkaline pH than that from C. albicans, and a half or a third of the specific activity of the C. albicans enzyme. These differences seemed to be associated with the difference of pathogenesis between Candida species. Of the 31 N-terminal amino acids, the enzymes of these three Candida species revealed 12 homologous amino acids.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Candida / enzymology*
  • Candida albicans / enzymology*
  • Electrophoresis, Polyacrylamide Gel
  • Endopeptidases / chemistry*
  • Endopeptidases / metabolism
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Isoelectric Point
  • Molecular Sequence Data
  • Molecular Weight
  • Sequence Homology, Amino Acid

Substances

  • Endopeptidases