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Enzymatic and biochemical characterization of Bungarus sindanus snake venom acetylcholinesterase
Provedor de dados: 80
Autores: Ahmed,M; Latif,N; Khan,RA; Ahmad,A; Rocha,JBT; Mazzanti,CM; Bagatini,MD; Morsch,VM; Schetinger,MRC.
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...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Acetylcholinesterase; Inhibition; Krait; Ionic strength; Acetylthiocholine iodide; Bungarus sindanus; Snake venom.
Ano: 2012
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000200014