Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography

Tan, C.H. and Sim, S.M. and Gnanathasan, C.A. and Fung, Shin Yee and Ponnudurai, G. and Pailoor, J. and Tan, N.H. (2011) Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography. Journal of Venomous Animals and Toxins including Tropical Diseases, 17 (4). pp. 473-485. ISSN 1678-9199

[img]
Preview
PDF
Enzymatic_and_toxinological_activities_of_Hypnale_hypnale_(hump-_nosed_pit_viper)_venom_and_its_fractionation_by_ion_exchange_high_performance_liquid_chromatography.pdf - Published Version

Download (576kB)

Abstract

Hypnale hypnale (hump-nosed pit viper) has been recently identified as one of the medically important venomous snakes in Sri Lanka and on the southwestern coast of India. The characterization of its venom is essential for understanding the pathophysiology of envenomation and for optimizing its management. In the present study, the biological properties of Hypnale hypnale venom and venom fractions obtained using Resource Q ion exchange chromatography were determined. The venom exhibited toxic activities typical of pit viper venom, comparable to that of its sister taxon, the Malayan pit viper (Calloselasma rhodostoma). Particularly noteworthy were its high activities of thrombin-like enzyme, proteases, phospholipase A2, L-amino acid oxidase and hyaluronidase. The thrombin-like enzyme was mainly acidic and distributed over several chromatography fractions, indicating its existence in multiple isoforms. The hemorrhagic and necrotic activities of the venom were likely associated with the proteolytic enzyme found mainly in the basic fraction. Phospholipase A2 and phosphomonoesterase exist in both acidic and basic isoforms, while L-amino acid oxidase and hyaluronidase are highly acidic. The venom clotting activity on fibrinogens showed distinct species specificity in the following increasing order for clotting time: bovine < rabbit < goat < human < horse < < dog, and was comparable to that of C. rhodostoma venom. Its clot formation on human fibrinogen is gradual and prolonged, a phenomenon suggestive of consumptive coagulopathy as a complication observed clinically. At an intramuscular sublethal dose, the venom did not cause acute kidney injury in a rodent model, contrary to the positive control group treated with Daboia russelii venom. Nephrotoxicity may result from higher venom doses in the context of coagulopathy, as a complication provoked by venom hematoxicity.

Item Type: Article
Additional Information: Department of Molecular Medicine, Faculty of Medicine Building, University of Malaya, 50603 Kuala Lumpur, MALAYSIA
Uncontrolled Keywords: Hypnale hypnale, venom, enzymes, toxins, fibrinogen, nephrotoxicity.
Subjects: R Medicine
Divisions: Faculty of Medicine
Depositing User: Fung Shin Yee
Date Deposited: 13 Sep 2012 02:19
Last Modified: 21 Mar 2019 06:26
URI: http://eprints.um.edu.my/id/eprint/3691

Actions (login required)

View Item View Item

Downloads

Downloads per month over past year