Some properties of two purified fibinolytic enzymes from Bacillus subtilis and B. polymyxa.
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.
D001407:Bacillus / Q000201:enzymology*; D001412:Bacillus subtilis / Q000201:enzymology*; D002850:Chromatography, Gel; D003300:Copper / Q000494:pharmacology; D005342:Fibrinolysis; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D013045:Species Specificity; D013379:Substrate Specificity; D013696:Temperature
D003300:Copper; D010447:Peptide Hydrolases