Purification and some properties of pure Cochliobolus lunatus fibrinolytic Enzyme
β Scribed by Ahmed F. Abdel-Fattah; Abdel-Mohsen S. Ismail
- Publisher
- John Wiley and Sons
- Year
- 1984
- Tongue
- English
- Weight
- 381 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0006-3592
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## Abstract A fibrinolytic enzyme obtained from __B. subtilis__ was purified, using DEAEβcellulose column chromatography, and gel filtration on Sephadex Gβ100. The preparation was homogeneous as tested by gel filtration on Sephadex Gβ200, and disc electrophoresis. The molecular weight of this enzy
## 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 weigh