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Purification and properties of a fibrinolytic enzyme from Bacillus subtilis
Author(s) -
Fayek K. I.,
ElSayed Sanaa T.
Publication year - 1980
Publication title -
zeitschrift für allgemeine mikrobiologie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0044-2208
DOI - 10.1002/jobm.19800200603
Subject(s) - sephadex , size exclusion chromatography , bacillus subtilis , chromatography , chemistry , enzyme , enzyme assay , electrophoresis , cellulose , biochemistry , biology , bacteria , genetics
A fibrinolytic enzyme obtained from B. subtilis was purified, using DEAE‐cellulose column chromatography, and gel filtration on Sephadex G‐100. The preparation was homogeneous as tested by gel filtration on Sephadex G‐200, and disc electrophoresis. The molecular weight of this enzyme was 29.400 estimated by gel filtration on Sephadex G‐100. The optimum pH for enzyme activity was 7.2. Copper ions significantly increased enzyme activity, while Zn ++ and Mn ++ caused marked inhibition.