Gomes A, De P
Laboratory of Toxinology and Experimental Pharmacodynamics, Department of Physiology, University of Calcutta, 92, A.P.C. Road, Calcutta, 700 009, India.
Biochem Biophys Res Commun. 1999 Dec 20;266(2):488-91. doi: 10.1006/bbrc.1999.1818.
A novel fibrinolytic peptide (Hannahpep) was isolated and purified from the venom of the Indian King Cobra (Ophiophagus hannah) by thin-layer chromatography followed by reverse-phase high-performance liquid chromatography. The MW of the peptide was found to be 610 Da and the amino acid sequence of Hannahpep was determined to be Arg, His, Ala, Arg, His, Asp. Hannahpep produced defibrinogenating activity in male albino mice. It exhibited significant fibrinolytic and fibrinogenolytic activity in vitro. Hannahpep showed plasma-anticlotting activity. However, it lacked hemolytic, hemorrhagic, or phospholipase activity. This peptide may have possible therapeutic application in the management of thrombosis or occlusion of a blood vessel.