1980
DOI: 10.1002/jobm.3630200603
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Purification and properties of a fibrinolytic enzyme fromBacillus subtilis

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 enzyme was 29.400 estimated by gel filtration on Sephadex G-100. The optimum pH for enzyme activity was 7.2 Copper ions significantly increased enzyme activity, while Zn++ and Mn++ caused marked inhibition.

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Cited by 19 publications
(5 citation statements)
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“…Acetylcholinesterase (AChE) inhibitory activity was measured spectrophotometrically using the technique of Ellman et al [24]. Fibrinolytic activity was also assayed by the method of Fayek and El-Sayed [25]. …”
Section: Methodsmentioning
confidence: 99%
“…Acetylcholinesterase (AChE) inhibitory activity was measured spectrophotometrically using the technique of Ellman et al [24]. Fibrinolytic activity was also assayed by the method of Fayek and El-Sayed [25]. …”
Section: Methodsmentioning
confidence: 99%
“…Fibrinolytic activity was assayed by the method of Fayek and El-Sayed [10]. Each sample of 0.5 mL was added to 3 mL of a substrate solution (0.6% fibrin in 0.1M Mcllvaine buffer, pH 7.0) and incubated at 40℃ for 10 min.…”
Section: Methodsmentioning
confidence: 99%
“…Fibrinolytic activity was assayed by the method of Fayek and El-Sayed [24]. We added 0.5 mL of each sample to 3 mL of the substrate solution (0.6% fibrin in 0.1M McIlvaine buffer, pH 7.0) and incubated them at 40℃ for 10 min.…”
Section: Methodsmentioning
confidence: 99%