Enzymatic and biochemical characterization of Bungarus sindanus snake venom acetylcholinesterase
2012
Ahmed, M(University of Science and Technology Department of Biotechnology) | Latif, N(Federal University of Santa Maria Center of Natural and Exact Sciences Department of Biochemistry and Toxicology) | Khan, RA(University of Science and Technology Department of Biotechnology) | Ahmad, A(University of Science and Technology Department of Biotechnology) | Rocha, JBT(Federal University of Santa Maria Center of Natural and Exact Sciences Department of Biochemistry and Toxicology) | Mazzanti, CM(Federal University of Santa Maria Center of Natural and Exact Sciences Department of Biochemistry and Toxicology) | Bagatini, MD(Federal University of Santa Maria Center of Natural and Exact Sciences Department of Biochemistry and Toxicology) | Morsch, VM(Federal University of Santa Maria Center of Natural and Exact Sciences Department of Biochemistry and Toxicology) | Schetinger, MRC(Federal University of Santa Maria Center of Natural and Exact Sciences Department of Biochemistry and Toxicology)
This study analyses venom from the elapid krait snake Bungarus sindanus, which contains a high level of acetylcholinesterase (AChE) activity. The enzyme showed optimum activity at alkaline pH (8.5) and 45ºC. Krait venom AChE was inhibited by substrate. Inhibition was significantly reduced by using a high ionic strength buffer; low ionic strength buffer (10 mM PO4 pH 7.5) inhibited the enzyme by 1. 5mM AcSCh, while high ionic strength buffer (62 mM PO4 pH 7.5) inhibited it by 1 mM AcSCh. Venom acetylcholinesterase was also found to be thermally stable at 45ºC; it only lost 5% of its activity after incubation at 45ºC for 40 minutes. The Michaelis-Menten constant (Km) for acetylthiocholine iodide hydrolysis was found to be 0.068 mM. Krait venom acetylcholinesterase was also inhibited by ZnCl2, CdCl2, and HgCl2 in a concentrationdependent manner. Due to the elevated levels of AChE with high catalytic activity and because it is more stable than any other sources, Bungarus sindanus venom is highly valuable for biochemical studies of this enzyme.
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