一种酶对不稳定底物的米氏常数（Km）和最大反应速度（V）的测定及其在醛脱氢酶催化N τ-甲基咪唑-3-基乙醛氧化反应中的应用
Determination of Km and V of an enzyme for an unstable substrate and its application to the oxidation of N tau-methylimidazol-3-ylacetaldehyde by aldehyde dehydrogenase.
作者信息
Gitomer W L, Tipton K F
出版信息
Biochem J. 1983 Apr 1;211(1):277-80. doi: 10.1042/bj2110277.
The method of Storer & Cornish-Bowden [(1974) Biochem. J. 141, 205-209] for determining the lag time in coupled enzyme assays was adapted to enable the kinetic parameters of the second (coupling) enzyme for the intermediate to be calculated. The validity and accuracy of this method of progress-curve analysis was established by comparing the Km value of glucose 6-phosphate dehydrogenase for glucose 6-phosphate generated in situ by the action of glucose phosphate isomerase on fructose 6-phosphate with that determined from initial-rate measurements. The method was applied to the determination of the Km value of ox liver cytoplasmic aldehyde dehydrogenase for N tau-methylimidazol-3-ylacetaldehyde that was generated in situ by the action of plasma amine oxidase on N tau-methylhistamine.
斯托勒和康沃尔-鲍登（1974年，《生物化学杂志》第141卷，205 - 209页）测定偶联酶分析中延滞时间的方法经过改进，以便能够计算第二种（偶联）酶对中间产物的动力学参数。通过比较磷酸葡萄糖异构酶作用于6 - 磷酸果糖原位生成的6 - 磷酸葡萄糖的葡萄糖6 - 磷酸脱氢酶的Km值与通过初速率测量确定的Km值，确定了这种进程曲线分析方法的有效性和准确性。该方法被应用于测定牛肝细胞质醛脱氢酶对血浆胺氧化酶作用于Nτ - 甲基组胺原位生成的Nτ - 甲基咪唑 - 3 - 基乙醛的Km值。
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