Malakhov V N, Tishchenko V A, Efron I I, Chukhriĭ E A, Isachenkov V A
Biokhimiia. 1977 Jul;42(7):1221-31.
Properties of human creatine kinase isoenzymes (MM, MB and BB) are investigated. The most pronounced differences in properties of these isoenzymes are found under their urea inactivation, heat denaturation and the inhibition by rabbit antisera to isoenzymes. Differences in values of the Mikhaelis constant and substrate and pH dependencies are much less pronounced. The presence of ADP stabilizes creatine kinase isoenzymes under conditions of urea and heat inactivation. Properties of hybrid MB isoenzymes are found to be intermediate with respect to MM and BB isoenzymes. A mode of the interaction of M and B subunits in dimeric molecules of creatine kinase isoenzymes is discussed.
对人肌酸激酶同工酶（MM、MB和BB）的特性进行了研究。这些同工酶在尿素失活、热变性以及兔抗同工酶血清抑制作用下，其特性差异最为显著。米氏常数、底物及pH依赖性的值的差异则不太明显。ADP的存在在尿素和热失活条件下可稳定肌酸激酶同工酶。发现杂合MB同工酶的特性在MM和BB同工酶之间呈中间状态。讨论了肌酸激酶同工酶二聚体分子中M和B亚基的相互作用模式。
