Journal
TOXIN REVIEWS
Volume 41, Issue 1, Pages 165-174Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15569543.2020.1855656
Keywords
Indian cobra; anticoagulant; serine protease; fibrinogenolytic
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Funding
- Visvesvaraya Technological University, Belgavi [VTU/Aca/2011 12/A-9/739]
- UGC, Govt of India [RGNF-SCKAR-7967]
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An unusual low molecular weight serine protease (NnP28) was purified from Indian Cobra venom. NnP28 exhibited proteolytic activity and anticoagulant properties, prolonging clotting time and inhibiting thrombin generation.
An unusual low molecular weight serine protease (NnP28) has been purified from Indian Cobra (Naja naja) venom from the western region of the Indian sub-continent. We reported the purification and characterization of low molecular NnP28, emphasizing its role on human fibrinogen and anticoagulant property. NnP28 was purified using gel filtration column chromatography followed by ion exchange chromatography. Protein gel electrophoresis revealed its molecular weight approximate to 28 kDa. The exact molecular mass of NnP28 was found to be 27.12 kDa by mass spectrometry, hydrolyzing casein specifically, inhibited by PMSF suggesting it has a serine protease. NnP28 prolonged the clotting time of re-calcified human citrated plasma and activated partial thromboplastin time (APTT) exhibiting anticoagulant property. NnP28 exhibited fibrinogenolytic activity. Thus, the present study demonstrates the presence of unusual low molecular weight serine protease, emphasizing its importance of region-specific Indian cobra species.
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