Serine protease from Indian Cobra venom: its anticoagulant property and effect on human fibrinogen

Abstract

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 ≈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.

Keywords:

• Indian cobra
• anticoagulant
• serine protease
• fibrinogenolytic

Disclosure statement

On behalf of all authors, the corresponding author states that there is no conflict of interest.

Additional information

Funding

SNS thanks Visvesvaraya Technological University, Belgavi for the financial assistance under VTU Research Grants vide no VTU/Aca/2011 12/A-9/739, dated 05-05-2012. NKN thanks UGC, Govt of India for UGC-RGNF [RGNF-SCKAR-7967, dt 06/06/2012] for awarding Junior and Senior Research Fellowship.