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Some properties of two purified fibrinolytic enzymes from Bacillus subtilis and B. polymyxa

✍ Scribed by Dr. K. I. Fayek; Sanaa T. El-Sayed

Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
303 KB
Volume
20
Category
Article
ISSN
0233-111X

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✦ Synopsis

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.

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