title: [Isolation of Bacillus thuringiensis IMV B-7324 fibrinolytic peptidase].
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.
authors.forename: N A
authors.initials: NA
authors.lastname: Nidialkova
authors.forename: O V
authors.initials: OV
authors.lastname: Matseliukh
authors.forename: L D
authors.initials: LD
authors.lastname: Varbanets'
mesh_terms: D000645:Ammonium Sulfate / Q000737:chemistry; D001413:Bacillus thuringiensis / Q000737:chemistry / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D005337:Fibrin / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000737:chemistry / Q000302:isolation & purification*
chemical_list: D001426:Bacterial Proteins; D003470:Culture Media; D005337:Fibrin; D010447:Peptide Hydrolases; D000645:Ammonium Sulfate