1887

Abstract

Summary

An elastase of was purified by ion exchange chromatography on CM-Sepharose and characterised. Its M is 21 kDa, its optimal temperature for activity is 42°C and the pH optimum is 6·8. The enzyme is activated by cysteine and other SH-donators and inhibited by l-trans-epoxy-succinylleucylamido-(4-guanidino)butane (E64), an inhibitor of cysteine proteases, but not by 3,4-dichloroisocoumarin (3,4-DCI), an inhibitor of serine proteases. This finding suggests that the elastase of is a cysteine protease. Because elastase degrades human sIgA, IgM, serum albumin, fibrinogen, and fibronectin, this enzyme may be regarded as a virulence factor.

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/content/journal/jmm/10.1099/00222615-37-3-201
1992-09-01
2019-10-20
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http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-37-3-201
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