Chemical studies on protease A of Bitis arietans (puff adder) venom |
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| Authors: | D J Strydom F J Joubert N L Howard |
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| Affiliation: | 1. Monash Venom Group, Department of Pharmacology, Faculty of Medicine, Nursing and Health Sciences, 3168 Clayton, Victoria, Australia;2. Jeffrey Cheah School of Medicine and Health Sciences, Monash University Malaysia, 46150 Bandar Sunway, Malaysia;3. Kulliyyah of Pharmacy, International Islamic University Malaysia, Kuantan Campus, Bandar Indera Mahkota, 25200 Kuantan, Pahang, Malaysia;4. Department of Pharmacology, Faculty of Medicine, University of Malaya, 59100 Kuala Lumpur, Malaysia |
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| Abstract: | Protease A of Bitis arietans venom is probably a metalloprotease, since it is inhibited by o-phenanthroline and contains 0.77 moles of zinc per mole protein. The enzyme comprises 213 amino acids, including 9 methionine residues and one free sulphydryl group. It contains one polypeptide chain, which is terminated at the carboxyl end by serine. The amino terminal sequence of protease A is: Arg-Ser-Ser-Asp-Pro-Asn-Lys-Tyr-Phe-Asn-Val-Ile-Val-Val-Val-Asp-Asn-Arg- Met-Val-Asn-Tyr-Tyr-Lys-Gly-Glu-Leu-Asn-Lys-Ile-Thr-. Despite difficulties with 'insoluble peptide core' formation, a number of peptides were purified from peptic and tryptic digests of S-derivatized protease A. |
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