The chemotactic activity of Candida albicans proteinase toward human peripheral leuko- cytes was examined by a modified Boyden chamber method.It was found that C.albicans proteinase in- duce dose-dependent chemotactic activity for neutrophils with maximal activity at 500 nmol/L(P

Candida albicans produced a karatinolytic proteinase (KPase) or C. albicans producing proteinase (CAPP), a proposed new term for this enzyme, and Trichophyton mentagrophytes also produced KPase when cultivated in liquid medium containing human stratum corneum (HSC) as the nitrogen source, but were unable to do so when cultivated in sabouraud dextrose broth. Purified KPase from the culture supernatants of C. albicans had a molecular weight of 42,000 and an optimum pH at 4.0. The KPase was found to belong to the carboxyl proteinases group and its activity was strongly inhibited by pepstatin. Both fungi were able to grow by secreting KPase which digested HSC for nutrients. KPase from both fungi had high activity in each optimum pH, such as weakly acidic pH on C. albicans and neutral pH on T. mentagrophytes to adapt their surrounding environment by changing the environmental pH into their own optimum pH.
Candida albicans/*enzymology/growth & development ; Culture Media ; Endopeptidases/*physiology ; Hydrogen-Ion Concentration ; Molecular Weight ; Trichophyton/*enzymology/growth & development