Yuu H, Takagi Y, Senju O, Hosoya J, Gomi K, Ishii T
Clin Chem. 1978 Nov;24(11):2054-7.
We describe an atypical serum creatine kinase isoenzyme in the serum of a woman with cancer of the left breast. This isoenzyme migrated toward the cathode, closely following the MM isoenzyme on agarose gel electrophoresis. Its relative molecular mass was estimated to be about 325,000, fourfold that of normal creatine kinase. It is more heat-stable and is inhibited more by urea than the normal MM isoenzyme. Isoenzyme monomer B activity was observed to be 20 U/liter in the serum, as measured with use of an antibody against the M monomer. On anion-exchange column analysis, creatine kinase activity was observed only in the MM fraction, in spite of the fact that B activity was observed in the patient's serum. Results of the immunological investigation make it unlikely that the atypical isoenzyme is linked to immunoglobulin or beta-lipoprotein. It may have been present as the result of modification of normal creatine kinase by the therapeutic radiation the patient was receiving.
我们描述了一名左乳癌女性血清中的一种非典型肌酸激酶同工酶。在琼脂糖凝胶电泳上，这种同工酶向阴极迁移，紧跟MM同工酶之后。其相对分子质量估计约为325,000，是正常肌酸激酶的四倍。它比正常的MM同工酶更耐热，且更易被尿素抑制。使用针对M单体的抗体检测发现，血清中同工酶单体B的活性为20 U/升。在阴离子交换柱分析中，尽管在患者血清中检测到了B活性，但肌酸激酶活性仅在MM组分中被观察到。免疫学研究结果表明，这种非典型同工酶不太可能与免疫球蛋白或β-脂蛋白有关。它可能是患者接受的治疗性放疗对正常肌酸激酶进行修饰的结果。
