Preparation and properties of fibrinolytic enzymes produced byCochliobolus lunatus
作者:
Ahmed F. Abdel‐Fattah,
Abdel Mohsen S. Ismail,
期刊:
Biotechnology and Bioengineering
(WILEY Available online 1984)
卷期:
Volume 26,
issue 1
页码: 37-40
ISSN:0006-3592
年代: 1984
DOI:10.1002/bit.260260108
出版商: Wiley Subscription Services, Inc., A Wiley Company
数据来源: WILEY
摘要:
AbstractSome properties of the crude lyophilized fibrinolytic enzyme produced byCochliobolus lunatusin surface culture were studied. Enzyme concentrations over the range from 0.16 to 10.16 mg/mL showed that concentration above a certain level ceased to be the limiting factor controlling enzyme action. At pH 6.8 and a temperature of 40°C, the fibrinolytic enzyme showed maximal activity at a human fibrin concentration of 2 mg/mL. The optimum pH values for enzyme activity were 6.98 and 7.0, using Sørensen and Mcllvaine buffers, respectively. Fibrinolytic enzymes were isolated from a static culture ofCochliobolus lunatus; isolation was carried out with various agents. Ammonium sulphate yielded the highest recovered fibrinolytic activity. The fraction salted out by precipitation at 25% ammonium sulphate saturation possessed the highest recovered fibrinolytic activity compared to the ammonium sulphate, ethanol, and acetone fraction
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