Alvarez F V, Geijo S A, Sánchez A C, Dopico M T, Bao C G
Clin Biochem. 1983 Oct;16(5):299-302. doi: 10.1016/s0009-9120(83)94109-7.
We describe the abnormal electrophoretic mobility of a creatine kinase isoenzyme in the serum of an apparently healthy individual. In agarose gel electrophoresis this isoenzyme migrates more toward the cathode than does the MM isoenzyme. It is more resistant to heat and more strongly inhibited by urea than the normal MM isoenzyme. We performed gel filtration, on a Sephadex G-200 column, of the patient's serum and observed two distinct isoenzymes with different relative molecular masses; a normal isoenzyme of 80,000 daltons and another abnormal one of 240,000 daltons. We performed serum immunoelectrophoresis but did not observe any immune complex formation involving the abnormal isoenzyme.
我们描述了一名看似健康个体血清中肌酸激酶同工酶异常的电泳迁移率。在琼脂糖凝胶电泳中，这种同工酶比MM同工酶更向阴极迁移。与正常的MM同工酶相比，它对热更具抗性，且更易被尿素强烈抑制。我们在Sephadex G - 200柱上对患者血清进行了凝胶过滤，观察到两种具有不同相对分子质量的不同同工酶；一种是80,000道尔顿的正常同工酶，另一种是240,000道尔顿的异常同工酶。我们进行了血清免疫电泳，但未观察到涉及异常同工酶的任何免疫复合物形成。
