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- W1978752905 abstract "Acetylcholinesterase from Bungarus fasciatus venom has been prepared free of electrophoretically or immunologically detectable contaminating proteins. A specific activity of 270 mmol acetylcholine hydrolysed per h per mg was observed for the homogenous enzyme. A molecular weight of 126000 as determined by sedimentation and diffusion, has been found. The enzyme is split into two apparently equal‐sized subunits by 8M urea—1 M NaCl. Active‐site measurements revealed two active sites per enzyme molecule. The enzyme exhibited substrate inhibition and had a K m of 141.7 μM for acetylcholine. The enzyme was not inhibited by phenylmethylsulfonyl fluoride." @default.
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- W1978752905 date "1973-05-01" @default.
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- W1978752905 title "The Acetylcholinesterase of Bungarus fasciatus Venom" @default.
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- W1978752905 doi "https://doi.org/10.1111/j.1432-1033.1973.tb02799.x" @default.
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