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J Med Microbiol. 1995 Oct;43(4):282-8.

Purification and characterisation of a metallopeptidase of Candida albicans.

Author information

1
Laboratoire de Parasitologie et Mycologie M├ędicales, Centre Hospitalier Universitaire La Mil├ętrie, Poitiers, France.

Abstract

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.

PMID:
7562990
DOI:
10.1099/00222615-43-4-282
[Indexed for MEDLINE]

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