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The Journal of Medical Microbiology, Vol 43, Issue 4 282-288, Copyright © 1995 by Society for General Microbiology

JOURNAL ARTICLE

Purification and characterisation of a metallopeptidase of Candida albicans

B. el Moudni, M. H. Rodier, C. Barrault, M. Ghazali and J. L. Jacquemin
Laboratoire de Parasitologie et Mycologie Medicales, Centre Hospitalier Universitaire La Miletrie, Poitiers, France.

A novel aminopeptidase was purified by high performance liquid chromatography from a cytosoluble 100,000 g extract of Candida albicans on the basis of its ability to cleave L-arginine 7-amino-4-methylcoumarin. The purification factor was 36 and the yield was 20%. The native enzyme had a mol. wt of 52 kDa as demonstrated by SDS-PAGE in the presence or absence of reducing conditions and exhibited an iso-electric point of 4.3. The aminopeptidase showed optimum activity at pH 7.2, a Michaelis constant of c. 50 microM and a Vmax at 19 mM AMC released/min/mg of protein for L-Arg-AMC. This enzyme was shown to cleave at low affinity L-leucine-7-amino-4-methylcoumarin as demonstrated by the spectrofluorimetric method. The enzyme was strongly inhibited by specific metallo-enzyme inhibitors-EDTA and o-phenanthroline. Furthermore, there is evidence that a similar or identical enzyme occurs in other C. albicans clinical isolates and other Candida spp.


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