Exploring a new serine protease from cucumis sativus l

Nafeesa, Z. and Shivalingu, B. R. and Vivek, H. K. and Priya, B. S. and Swamy, S. N. (2015) Exploring a new serine protease from cucumis sativus l. APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 175 (6). pp. 2787-2794. ISSN 1559-0291

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Official URL: https://doi.org/10.1007/s12010-014-1462-5


Coagulation is an important physiological process in hemostasis which is activated by sequential action of proteases. This study aims to understand the involvement of aqueous fruit extract of Cucumis sativus L. (AqFEC) European burp less variety in blood coagulation cascade. AqFEC hydrolyzed casein in a dose-dependent manner. The presence of protease activity was further confirmed by casein zymography which revealed the possible presence of two high molecular weight protease(s). The proteolytic activity was inhibited only by phenyl methyl sulphonyl fluoride suggesting the presence of serine protease(s). In a dose-dependent manner, AqFEC also hydrolysed A alpha and B beta subunits of fibrinogen, whereas it failed to degrade the gamma subunit of fibrinogen even at a concentration as high as 100 mu g and incubation time up to 4 h. AqFEC reduced the clotting time of citrated plasma by 87.65 %. The protease and fibrinogenolytic activity of AqFEC suggests its possible role in stopping the bleeding and ensuing wound healing process.

Item Type: Article
Subjects: C Chemical Science > Chemistry
Divisions: Department of > Chemistry
Depositing User: Users 19 not found.
Date Deposited: 13 Jun 2019 10:41
Last Modified: 13 Jun 2019 10:41
URI: http://eprints.uni-mysore.ac.in/id/eprint/2776

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