1887

Abstract

Summary

secreted an inducible alkaline protease (AIPase) when cultivated in the presence of collagen (200 μg/ml) as sole nitrogen and carbon source. Proteolytic activity was maximum at pH 9.0 with azocollagen as substrate. The enzyme, which was the major protein found in the supernate of a liquid culture, was purified by ammonium sulphate precipitation and gel filtration. The Mr was determined to be 33 Kda by gel filtration and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The isoelectric point was estimated to be pH 8.2. Divalent cations strongly inhibited enzyme activity, whereas non-ionic detergents and reducing agents had no effect. AlPase was totally inhibited by phenylmethanesulphonyl fluoride, antipain, chymostatin and α-2-macroglobulin. AlPase is closely related to the AlPase, a serine protease of the subtilisin family, as attested by the antigen pattern seen by immunoblotting. The high collagenic activity and the ability of AlPase to digest elastin could play a role in the invasion of the tissues by the fungus.

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1991-07-01
2022-01-28
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