A cholinesterase was partially purified from bush bean (Phaseolus vulgaris L.) roots by using acridinium-based ligand affinity chromatography. The procedure gave a 78-fold increase in specific activity, although at least three inactive contaminants remained. The enzyme activity was maximal against acetyl esters of choline and was inhibited by neostigmine. Di-isopropyl phosphorofluoridate completely inhibited activity at concentrations greater than 0.1 mM. The catalytic centre activity was 2 × 10(-4) times that of electric eel acetylcholinesterase. Cholinesterase activity appeared as a peak (s = 4.2 +/- 0.1 S) after isokinetic sedimentation. The Stokes radius was 4.00 nm and the apparent molecular weight was 72700 +/- 1900. The smallest active and native form of the enzyme appeared to be a monomer. This contrasts with animal acetylcholinesterases, in which the smallest active and native forms are multimeric.
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December 1978
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Research Article|
December 01 1978
Partial purification and some properties of a cholinesterase from bush bean (Phaseolus vulgaris L.) roots
Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1978 London: The Biochemical Society
1978
Biochem J (1978) 175 (3): 769–777.
Citation
D H Mansfield, G Webb, D G Clark, I E P Taylor; Partial purification and some properties of a cholinesterase from bush bean (Phaseolus vulgaris L.) roots. Biochem J 1 December 1978; 175 (3): 769–777. doi: https://doi.org/10.1042/bj1750769d
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