Malakhov V N, Tishchenko V A, Isachenkov V A
Biokhimiia. 1978 Dec;43(12):2211-21.
The interaction of human creatine phosphokinase isoenzymes with rabbit antibodies and their Fab has been studied. It has been shown that Fab of the antibodies against MM or BB isoenzymes preserve high specificity of intact antibodies and the ability to inhibit creatine kinase isoenzymes. Differences between antibodies and their Fab have been found to exist with respect to the kinetics of binding with homologous isoenzymes: the rate of the complex formation for Fab is significantly higher. The interaction of creatine kinase isoenzymes with intact antibodies and their Fab is not affected by the addition of creatine kinase substrates. The antibodies against MM and BB isoenzymes have been used to study the individual properties of each subunit of the M- and B-type in a hybrid dimer MB. It has been shown that such properties of these subunits as the Michaelis constants, pH dependence and inhibition by homologous antibodies are identical to those of non-hybrid MM and BB isoenzymes, respectively.
已对人肌酸磷酸激酶同工酶与兔抗体及其Fab片段的相互作用进行了研究。结果表明，针对MM或BB同工酶的抗体的Fab片段保留了完整抗体的高特异性以及抑制肌酸激酶同工酶的能力。已发现抗体及其Fab片段在与同源同工酶结合的动力学方面存在差异：Fab片段形成复合物的速率明显更高。肌酸激酶同工酶与完整抗体及其Fab片段的相互作用不受肌酸激酶底物添加的影响。针对MM和BB同工酶的抗体已用于研究杂合二聚体MB中M型和B型各亚基的个体特性。结果表明，这些亚基的米氏常数、pH依赖性以及同源抗体的抑制等特性分别与非杂合MM和BB同工酶的特性相同。
