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 Km of 141.7 μM for acetylcholine. The enzyme was not inhibited by phenylmethylsulfonyl fluoride.
No takes yet. Share an insight, caveat, or question.
Kumar et al. (1973) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: