Homburger H A, Wold L, Jacob G L, O'Brien J
Clin Chem. 1980 Jan;26(1):78-83.
Metastable creatine kinase MM isoenzyme was isolated and partially purified from homogenates of myocardium and skeletal muscle by gradient elution on carboxymethyl cellulose. This variant isoenzyme migrated between the MM and MB isoenzymes on agarose electrophoresis, accounted for 3.5% of the total creatine kinase activity in each tissue, was not a macromolecule, and had stable electrophoretic mobility only in borate buffer (0.02 mol/L). By comparison, the creatine kinase isoenzymes with similar "atypical" electrophoretic mobility in serum specimens were complexes of the BB isoenzyme and immunoglobulin G. These complexes were measured by a radioimmunoassay specific for the creatine kinase B-subunit and eluted predominantly with the MB isoenzyme in a commercial anion-exchange reagent system.
通过羧甲基纤维素梯度洗脱，从心肌和骨骼肌匀浆中分离并部分纯化了亚稳肌酸激酶MM同工酶。这种变异同工酶在琼脂糖电泳中迁移于MM和MB同工酶之间，在每个组织中占总肌酸激酶活性的3.5%，不是大分子，且仅在硼酸盐缓冲液（0.02 mol/L）中具有稳定的电泳迁移率。相比之下，血清标本中具有类似“非典型”电泳迁移率的肌酸激酶同工酶是BB同工酶与免疫球蛋白G的复合物。这些复合物通过针对肌酸激酶B亚基的放射免疫测定法进行检测，并在商业阴离子交换试剂系统中主要与MB同工酶一起洗脱。
