乙酰胆碱酯酶中催化位点的数量。
The number of catalytic sites in acetylcholinesterase.
作者信息
Leuzinger W
出版信息
Biochem J. 1971 Jun;123(2):139-41. doi: 10.1042/bj1230139.
Abstract
By using two methods of titration, the number of active sites in acetylcholinesterase was determined. Either stepwise inhibition of the enzyme by an irreversible inhibitor, namely di-isopropyl phosphorofluoridate, or direct measurement of the concentration of active sites by titration with o-nitrophenyl dimethylcarbamate yielded an equivalent weight of approx. 130000 for an active site in acetylcholinesterase. This indicates two sites per molecule, since the native enzyme has a molecular weight of 260000.
摘要
通过两种滴定方法，测定了乙酰胆碱酯酶中的活性位点数量。用不可逆抑制剂二异丙基氟磷酸酯逐步抑制该酶，或用邻硝基苯基二甲基氨基甲酸酯滴定直接测量活性位点的浓度，结果显示乙酰胆碱酯酶中一个活性位点的当量约为130000。由于天然酶的分子量为260000，这表明每个分子有两个位点。
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本文引用的文献
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Acetylcholinesterase, I. Large-scale purification, homogeneity, and amino Acid analysis.乙酰胆碱酯酶，I. 大规模纯化、均一性及氨基酸分析。
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