单甲基氨基甲酸酯对红细胞胆碱酯酶的抑制动力学
The kinetics of inhibition of erythrocyte cholinesterase by monomethylcarbamates.
作者信息
Reiner E, Simeon-Rudolf V
出版信息
Biochem J. 1966 Feb;98(2):501-5. doi: 10.1042/bj0980501.
Abstract
- The kinetics of the interaction of erythrocyte cholinesterase with 1-naphthyl N-methylcarbamate, 2-isopropoxyphenyl N-methylcarbamate and phenyl N-methylcarbamate were studied. Rate constants for inhibition and rate constants for spontaneous reactivation were determined. The calculated rate constants for spontaneous reactivation agreed well with those obtained experimentally. 2. The degree of inhibition obtained after preincubation of enzyme and inhibitor was found to be independent of both the substrate concentration and the dilution of the inhibited enzyme. 3. The reaction between the enzyme and the inhibitor was consistent with carbamates being regarded as poor substrates of cholinesterases. There was no evidence for the formation of a reversible complex between the enzyme and the carbamate.
摘要
- 研究了红细胞胆碱酯酶与1-萘基N-甲基氨基甲酸酯、2-异丙氧基苯基N-甲基氨基甲酸酯和苯基N-甲基氨基甲酸酯相互作用的动力学。测定了抑制速率常数和自发重新激活速率常数。计算得到的自发重新激活速率常数与实验获得的结果吻合良好。2. 发现酶和抑制剂预孵育后获得的抑制程度与底物浓度和被抑制酶的稀释度均无关。3. 酶与抑制剂之间的反应符合将氨基甲酸酯视为胆碱酯酶不良底物的情况。没有证据表明酶与氨基甲酸酯之间形成了可逆复合物。
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本文引用的文献
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Some properties of specific cholinesterase with particular reference to the mechanism of inhibition by diethyl p-nitrophenyl thiophosphate (E 605) and analogues.特异性胆碱酯酶的某些特性，特别涉及对硫代磷酸O,O-二乙基对硝基苯酯（E605）及其类似物的抑制机制。
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A new and rapid colorimetric determination of acetylcholinesterase activity.一种新的快速比色法测定乙酰胆碱酯酶活性。
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Studies on cholinesterase. VIII. Determination of reaction velocity constants with a reversible inhibitor of pseudocholinesterase.胆碱酯酶研究。VIII. 用假性胆碱酯酶的可逆抑制剂测定反应速度常数。
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