Cholinesterases from Plant Tissue: V. Cholinesterase Is Not Pectin Esterase 1
AUTOR(ES)
Fluck, Richard A.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=366607Documentos Relacionados
- Cholinesterases from Plant Tissues: I. Purification and Characterization of a Cholinesterase from Mung Bean Roots 1
- Cholinesterases from Plant Tissues: II. Inhibition of Bean Cholinesterase by 2-Isopropyl-4-dimethylamino-5-methylphenyl-1-piperidine Carboxylate Methyl Chloride (AMO-1618) 1
- Gravitropism in Higher Plant Shoots 1: V. Changing Sensitivity to Auxin
- Phosphoenolpyruvate Carboxylase from Spinach Leaf Tissue: Inhibition by Sulfite Ion 1
- Cholinesterases from Plant Tissues: III. Distribution and Subcellular Localization in Phaseolus aureus Roxb. 1