Department of Botany, Ohio University, Athens, Ohio 45701.
Plant Physiol. 1974 Nov;54(5):797-8. doi: 10.1104/pp.54.5.797.
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 mum neostigmine, a potent inhibitor of the cholinesterase activity extracted from Phaseolus aureus.
对比了菜豆金雀异黄素和果胶（甲基）酯酶（来自菜豆金雀异黄素和番茄）的几种特性。胆碱酯酶活性被测试的所有浓度的 NaCl 抑制，从 0.05 m 到 0.9 m，这一特性与果胶酯酶的已发表数据有很大的不同。尽管粗制的胆碱酯酶制剂含有果胶酯酶活性，但通过凝胶过滤进一步纯化胆碱酯酶会导致果胶酯酶活性几乎完全消除。来自番茄的果胶酯酶和来自菜豆金雀异黄素的果胶酯酶的活性都不受 25 µm 新斯的明的影响，新斯的明是从菜豆金雀异黄素中提取的胆碱酯酶活性的强抑制剂。
