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- W1965602009 abstract "Abstract Acetylcholinesterase from Bungarus fasciatus venom has been purified by a conventional procedure with a specific activity of 230 millimoles acetylcholine hydrolysed mg protein−1 hr−1. The enzyme with a molecular weight of 126, 000 has an excess of acidic amino acids over basic amino acids. The N-terminal amino acid analysis gave leucine as the only N-terminal amino acid with a free amino group. There are no common antigenic sites between the B. fasciatus venom acetylcholinesterase and acetylcholinesterases from bovine erythrocytes and electric eel." @default.
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- W1965602009 title "Acetylcholinesterase from a Non-membrane Source (Bungarus fasciatus Venom)" @default.
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- W1965602009 doi "https://doi.org/10.1080/00327487308061539" @default.
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