1991
DOI: 10.1007/bf02885378
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Acetylcholinesterase from oat Seedlings. I. Preliminary biochemical characterization of the enzyme

Abstract: The activity of acetylcholinesterase (ACHE) isolated from coleoptiles of etiolated oat seedlings is strongly inhibited by neostigmine and less so by eserine. The optimum of the enzyme activity occurs at pH 7.2 and a temperature of + 36"C. The enzyme Michaelis constant is 280 laM. Choline within the range of concentration from 0.001 to 10 mM does not affect the enzyme activity. Calcium ions at 5 mM concentration cause inhibition, while magnesium and manganese ions do not affect the enzyme activity.AChE isolated… Show more

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Cited by 3 publications
(1 citation statement)
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“…These enzymes (specific acetylcholinesterases included) commonly appear in plant tissues (Miura andShih 1984, Tretyn andKendrick 1991). It is known that the degradation of choline esters in extracts may be effectively impeded by the inhibitors of AChE -eserine and neostigmine (K~sy et al 1991, Tretyn andKen-drick 1991). Since these inhibitors are structural analogues of ACh they undergo simultaneous precipitation with choline esters.…”
Section: Resultsmentioning
confidence: 99%
“…These enzymes (specific acetylcholinesterases included) commonly appear in plant tissues (Miura andShih 1984, Tretyn andKendrick 1991). It is known that the degradation of choline esters in extracts may be effectively impeded by the inhibitors of AChE -eserine and neostigmine (K~sy et al 1991, Tretyn andKen-drick 1991). Since these inhibitors are structural analogues of ACh they undergo simultaneous precipitation with choline esters.…”
Section: Resultsmentioning
confidence: 99%