Some properties of two purified fibrinolytic enzymes fromBacillus subtilis andB. polymyxa

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Abstract
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.