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Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993)

[Isolation of Bacillus thuringiensis IMV B-7324 fibrinolytic peptidase].


PMID 23120980

Abstract

Fibrinolytic peptidase of Bacillus thuringiensis IMV B-7324 was isolated by ammonium sulfate fractionation, gel-filtration and ion exchange chromatography on TSK-gels--Toyopearl HW-55 and DEAE 650 (M). Fibrinolytic activity of the purified enzyme was 87.9 U/mg of protein that was 19.9 times higher compared with the supernatant cultural liquid, the yield on its activity reached 31%. The gel-filtration on Sepharose 6B and by SDS-PAGE electrophoresis demonstrated the homogeneity of the purified fibrinolytic peptidase, which molecular weight was approximately 24 kDa.