| Literature DB >> 11998872 |
Masahiro Nishimura1, Hiroki Nikawa, Hirofumi Yamashiro, Haruki Nishimura, Taizo Hamada, Graham Embery.
Abstract
Cell associated collagenolytic activity of Candida albicans was quantified by measuring the degradation of synthetic peptide 2-furanacryloyl-Leu-Gly-Pro-Ala (FALGPA), which is a specific substrate for collagenase, by the freeze-thaw procedure method. This collagenolytic activity was enhanced by cells cultured in the presence of bovine serum albumin (BSA) in culture medium. However, this activity was inhibited in the presence of ethylenediaminetetraacetic acid disodium salt (EDTA-2Na), but not by the serine proteinase inhibitor p-amidinophenyl methanesulfonyl fluoride (APMSF), nor the aspartyl proteinase inhibitor pepstatin A. These results suggested the presence of a metalloenzyme on pericellular C. albicans.Entities:
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Year: 2002 PMID： 11998872 DOI： 10.1023/a:1014506115757
Source DB: PubMed Journal: Mycopathologia ISSN： 0301-486X Impact factor: 2.574