Nikol'skaia E B, Iagodina O V, Kostrova V M
Biokhimiia. 1982 Feb;47(2):290-5.
The dependency of initial rates of tyramine, tryptamine, serotonin and benzylamine reactions of deamination catalyzed by rat liver monoamine oxidase from its concentrations was studied potentiometrically using an air-gap electrode. The kinetic deamination parameters, i.e. Michaelis constants an maximum velocities, were determined at pH values of 7.6 and 9.0. The inhibition of tyramine deamination at high concentrations of the latter was found for a pH value of 9.0 and the activation of serotonin deamination by its high concentrations for pH values of 7.6 and 9.0. The effects studied may be interpreted in terms of the allosteric nature of MAO.
采用气隙电极通过电位分析法研究了大鼠肝脏单胺氧化酶催化的酪胺、色胺、5-羟色胺和苄胺脱氨反应的初始速率对其浓度的依赖性。在pH值为7.6和9.0时测定了动力学脱氨参数，即米氏常数和最大速度。发现在pH值为9.0时高浓度酪胺对酪胺脱氨有抑制作用，在pH值为7.6和9.0时高浓度5-羟色胺对5-羟色胺脱氨有激活作用。所研究的这些效应可以用单胺氧化酶的别构性质来解释。
