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Some properties of two purified fibrinolytic enzymes from Bacillus subtilis and B. polymyxa
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.19800200604
Subject(s) - bacillus subtilis , enzyme , sephadex , fibrin , paenibacillus polymyxa , size exclusion chromatography , chemistry , biochemistry , enzyme assay , chromatography , microbiology and biotechnology , biology , bacteria , immunology , genetics
Two fibrinolytic enzymes isolated from B. subtilis and from B. polymyxa were purified using a five step method. The pH optimum for the enzyme from B. subtilis was 7.2 and for the enzyme from B. polymyxa was 7.0. Both enzymes were activated by Cu ++ . The molecular weight of the first enzyme was 29,400 and that for the second enzyme was 18,000 on the basis of gel filtration on Sephadex G‐100. The enzyme from B. subtilis has higher affinity to buffalo fibrin than towards human fibrin. The enzyme from B. polymyxa has higher affinity to human fibrin than towards buffalo fibrin.