𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Purification and biochemical properties of a fibrinolytic enzyme from Bacillus subtilis-fermented red bean

✍ Scribed by Chen-Tien Chang; Pei-Ming Wang; Ya-Fang Hung; Yun-Chin Chung

Book ID
113626728
Publisher
Elsevier Science
Year
2012
Tongue
English
Weight
330 KB
Volume
133
Category
Article
ISSN
0308-8146

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Purification and properties of a fibrino
Purification and properties of a fibrinolytic enzyme from Bacillus subtilis
✍ Dr. K. I. Fayek; Sanaa T. El-Sayed πŸ“‚ Article πŸ“… 2007 πŸ› John Wiley and Sons 🌐 English βš– 404 KB

## Abstract A fibrinolytic enzyme obtained from __B. subtilis__ was purified, using DEAE‐cellulose column chromatography, and gel filtration on Sephadex G‐100. The preparation was homogeneous as tested by gel filtration on Sephadex G‐200, and disc electrophoresis. The molecular weight of this enzy

Some properties of two purified fibrinol
Some properties of two purified fibrinolytic enzymes from Bacillus subtilis and B. polymyxa
✍ Dr. K. I. Fayek; Sanaa T. El-Sayed πŸ“‚ Article πŸ“… 2007 πŸ› John Wiley and Sons 🌐 English βš– 303 KB

## 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

Purification and properties of milk-clot
Purification and properties of milk-clotting enzyme from Bacillus subtilis K-26
✍ Lavu Krishna Rao; D. K. Mathur πŸ“‚ Article πŸ“… 1979 πŸ› John Wiley and Sons 🌐 English βš– 524 KB

## Abstract A milk‐clotting enzyme from __Bacillus subtilis__ K‐26 was purified by gel filtration and ion‐exchange chromatography resulting in a 24‐fold increase in specific activity with an 80% yield. Polyacrylamide gel electrophoresis and ultracentrifugel analysis revealed that the purified enzym