Exploring a New Serine Protease from Cucumis sativus L View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2015-03

AUTHORS

Zohara Nafeesa, B. R. Shivalingu, H. K. Vivek, B. S. Priya, S. Nanjunda Swamy

ABSTRACT

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 Aα and Bβ subunits of fibrinogen, whereas it failed to degrade the γ subunit of fibrinogen even at a concentration as high as 100 μg 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. More... »

PAGES

2787-2794

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12010-014-1462-5

DOI

http://dx.doi.org/10.1007/s12010-014-1462-5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022325069

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25577345


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