Chemnitz G, Jockers-Wretou E, Schmidt E, Schmidt F W, Lobers J
J Clin Chem Clin Biochem. 1979 Nov;17(11):725-9. doi: 10.1515/cclm.1979.17.11.725.
From 2000 sera with elevated total creatine kinase (EC 2.7.3.2) activity the sera of 6 patient showed a persistent high and anamnestically inexplicable creatine kinase activity level. The serum isoenzyme pattern was analyzed by four different methods. Electrophoresis revealed an atypical creatine activity band located between creatine kinase-MM and creatine kinase-MB. An adequate estimation of the persistent enzyme activity could only be achieved by immunotitration (immunoprecipitation), which identified the creatine kinase activity as due primarily to the isoenzyme creatine kinase-BB. Other methods (immunoinhibition and column chromatography) may lead to misinterpretations. The atypical serum creatine kinase-BB showed a higher molecular weight (Mr = 250,000) and altered substrate affinity as compared to native creatine kinase-BB. Both properties are attributable to the binding of creatine kinase-BB to immunoglobulins.
在2000份总肌酸激酶（EC 2.7.3.2）活性升高的血清样本中，6例患者的血清显示出持续高且既往史无法解释的肌酸激酶活性水平。采用四种不同方法分析血清同工酶谱。电泳显示一条非典型肌酸活性带位于肌酸激酶-MM和肌酸激酶-MB之间。只有通过免疫滴定（免疫沉淀）才能对持续的酶活性进行充分评估，该方法确定肌酸激酶活性主要归因于同工酶肌酸激酶-BB。其他方法（免疫抑制和柱色谱法）可能会导致误解。与天然肌酸激酶-BB相比，非典型血清肌酸激酶-BB显示出更高的分子量（Mr = 250,000）和改变的底物亲和力。这两种特性均归因于肌酸激酶-BB与免疫球蛋白的结合。
