Massey T H, Butts W C
Clin Chem. 1983 Mar;29(3):533-8.
We have adapted to a microcentrifugal analyzer an immunoinhibition assay for measuring the activity of creatine kinase MB by using an inhibitory antibody for the M monomer. The method actually measures half the MB activity, but results are not multiplied by two because atypical isoenzymes of creatine kinase, including BB, IgG-BB, and the isoenzyme derived from mitochondria, are also detected, if they are present. Results correlated well with an electrophoresis method for 36 serum samples. Myocardial infarction was assessed in 175 patients admitted to our coronary-care unit, with respect to sensitivity (100%) and specificity (98%) when a decision point of 100 U/L (30 degrees C) was chosen for total creatine kinase activity (dithiothreitol-activated) and 6 U/L (30 degrees C) for the isoenzyme (by immunoinhibition). Atypical isoenzymes are easily recognized and confirmed by electrophoresis when the MB activity (by immunoinhibition) exceeds 6 U/L and 20% of the total creatine kinase activity.
我们对微量离心分析仪进行了改良，采用针对M单体的抑制性抗体，建立了一种免疫抑制测定法来检测肌酸激酶MB的活性。该方法实际测定的是MB活性的一半，但结果无需乘以2，因为如果存在非典型肌酸激酶同工酶，包括BB、IgG-BB以及线粒体来源的同工酶，也能被检测出来。对36份血清样本的检测结果与电泳法高度相关。对收入我们冠心病监护病房的175例患者进行心肌梗死评估时发现，当选择总肌酸激酶活性（二硫苏糖醇激活）的判定点为100 U/L（30℃）、同工酶（通过免疫抑制法）的判定点为6 U/L（30℃）时，该方法的敏感性为100%，特异性为98%。当MB活性（通过免疫抑制法）超过6 U/L且占总肌酸激酶活性的20%时，非典型同工酶很容易通过电泳识别并确认。
