人肌酸磷酸激酶同工酶的动力学特性
Kinetic properties of the isoenzymes of human creatine phosphokinase.
作者信息
Witteveen S A, Sobel B E, DeLuca M
出版信息
Proc Natl Acad Sci U S A. 1974 Apr;71(4):1384-7. doi: 10.1073/pnas.71.4.1384.
Abstract
Studies of the three human creatine phosphokinase (EC 2.7.3.2) isoenzymes, MM, MB, and BB, show that important differences exist in substrate dependency of the reaction rates. A method was developed to study these properties in which the ATP formed in the reverse reaction was measured by means of firefly luciferase. With substrate conditions at which the isoenzymes showed substantial differences in activity the method could be used for the detection of changes in the isoenzyme pattern of the serum of patients with an acute myocardial infarction. The MB isoenzyme appearing in this condition could be detected quantitatively.
摘要
对三种人类肌酸磷酸激酶（EC 2.7.3.2）同工酶MM、MB和BB的研究表明，反应速率的底物依赖性存在重要差异。开发了一种研究这些特性的方法，其中通过萤火虫荧光素酶测量逆反应中形成的ATP。在同工酶活性表现出显著差异的底物条件下，该方法可用于检测急性心肌梗死患者血清同工酶模式的变化。在这种情况下出现的MB同工酶可以进行定量检测。
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