Purification, characterization, and chemical modification of neurotoxic peptide from daboia russelii snake venom of india

Venkatesh, M. and Prasad, N. and Sing, T. and Gowda, V. (2013) Purification, characterization, and chemical modification of neurotoxic peptide from daboia russelii snake venom of india. Journal of Biochemical and Molecular Toxicology, 27 (6). pp. 295-304. ISSN 1095-6670

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Official URL: http://doi.org/10.1002/jbt.21486


Comprehensive knowledge of venom composition is very important for effective management of snake envenomation and antivenom preparation. Daboia russelii venom from the eastern region of India is the most neurotoxic among the four venom samples investigated. From the eastern D. russelii venom sample, neurotoxic peptide has been purified by combined method of ion exchange gel permeation chromatography and reversed phase high performance liquid chromatography. Molecular weight of Daboia neurotoxin III (DNTx-III) found to be 6,849 Da (as measured on matrix-assisted laser desorption/ionisation-time of flight mass spectrometer), and N-terminal amino acid sequences is I K C F I T P D U T S Q A. Approximate LD50 dosage was 0.24 mg/kg body weight. It produced concentration- and time-dependent inhibition of indirectly stimulated twitches of Rana hexadactyla sciatic nerve gastrocnemius muscle preparations. Chemical modification of DNTx-III tryptophan residue(s) reduced the twitch height inhibition property of toxin, signifying the importance of tryptophan residues for the neurotoxic function. This type of neurotoxic peptide is unique to east Indian regional D. russelii venom.

Item Type: Article
Uncontrolled Keywords: amino acid sequence, Amino Acid Sequence, animal experiment, Animals, Anura, article, chick, Chickens, concentration response, Daboia, Daboia russellii, Female, gastrocnemius muscle, Humans, India, LD 50, Lethal Dose 50, male, Male, Mice, molecular weight, Molecular Weight, mouse, Neuromuscular Junction, neurotoxin, Neurotoxins, nonhuman, Peptides, protein analysis, protein degradation, protein modification, protein purification, Rana hexadactyla, Ranidae, Russell's Viper, sciatic nerve, Snake Bites, snake venom, snake venom antiserum, survival time, tryptophan, Tryptophan, Viper Venoms, Viperinae
Subjects: C Chemical Science > Biochemistry
Divisions: Department of > Biochemistry
Depositing User: Arshiya Kousar
Date Deposited: 14 Nov 2019 05:49
Last Modified: 14 Nov 2019 05:49
URI: http://eprints.uni-mysore.ac.in/id/eprint/9610

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