Open AccessPurification and characterisation of elastase from Staphylococcus epidermidis
Author(s) -
N. Sloot,
Mitchell A. Thomas,
R Marre,
Sören Gatermann
Publication year - 1992
Publication title -
journal of medical microbiology/journal of medical microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.91
H-Index - 117
eISSN - 1473-5644
pISSN - 0022-2615
DOI - 10.1099/00222615-37-3-201
Subject(s) - proteases , elastase , staphylococcus epidermidis , pancreatic elastase , enzyme , cysteine , fibrinogen , biochemistry , chemistry , serine protease , protease , microbiology and biotechnology , virulence factor , serine , staphylococcus aureus , biology , bacteria , virulence , gene , genetics
An elastase of Staphylococcus epidermidis was purified by ion exchange chromatography on CM-Sepharose and characterised. Its M(r) is c. 21 kDa, its optimal temperature for activity is 42 degrees 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 S. epidermidis is a cysteine protease. Because S. epidermidis elastase degrades human sIgA, IgM, serum albumin, fibrinogen, and fibronectin, this enzyme may be regarded as a virulence factor.