pH-dependent denaturation of extracellular aspartic proteinases from Candida species.
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.
Department of Medical Microbiology, University of Göttingen, Germany.
T
T
Wagner
M
M
Borg von Zepelin
R
R
Rüchel
D016282:Aspartic Acid Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D002175:Candida / Q000145:classification / Q000201:enzymology* / Q000472:pathogenicity; D002176:Candida albicans / Q000201:enzymology / Q000472:pathogenicity; D002848:Chromatography, DEAE-Cellulose; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011489:Protein Denaturation; D012703:Serotyping; D013045:Species Specificity; D014774:Virulence
D016282:Aspartic Acid Endopeptidases