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. 1974 Nov;54(5):797–798. doi: 10.1104/pp.54.5.797

Cholinesterases from Plant Tissue

V. Cholinesterase Is Not Pectin Esterase 1

Richard A Fluck a, Mark J Jaffe a
PMCID: PMC366607  PMID: 16658976

Abstract

Several properties of the cholinesterase from Phaseolus aureus Roxb. and of pectin (methyl) esterases from both Phaseolus aureus and Lycopersicon esculentum (L.) Mill. are contrasted. Cholinesterase activity is inhibited by all of the concentrations of NaCl tested, from 0.05 m to 0.9 m, a property which differs sharply from published data pertaining to pectin esterase. Although crude preparations of cholinesterase contain pectin esterase activity, further purification by gel filtration of the cholinesterase results in a nearly complete elimination of the pectin esterase activity. The activity of neither the pectin esterase from Lycopersicon esculentum nor that from Phaseolus aureus is affected by 25 μm neostigmine, a potent inhibitor of the cholinesterase activity extracted from Phaseolus aureus.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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