Lahet C, Vialle A, Maire I, Parrin B, Steghens J P, Mathieu M
Clin Chem. 1986 Feb;32(2):271-4.
Whereas univariate studies led to an European agreement for the choice of optimal reagent concentrations of 2 mmol/L for ADP and 10 mmol/L for Mg2+ for determining creatine kinase (EC 2.7.3.2) activity in serum, whatever its isoenzyme pattern, the results of our bivariate study led us to recommend higher optimal concentrations: 4.1 to 4.7 mmol/L for ADP and 22 mmol/L for Mg2+. The zone of maximal activity was in fact a broad plateau such that more than 99% of maximal enzyme activity was attained at ADP concentrations between 3 and 5 mmol/L and Mg2+ concentrations between 17 and 26 mmol/L. Under these new conditions the maximum activity measured was modestly increased (about 10%) over the previously recommended method but the assay could be expected to be more resistant to the variations of ADP and Mg2+ concentrations. It may become necessary to modify the European recommended method.
尽管单变量研究促使欧洲达成共识，即无论血清肌酸激酶（EC 2.7.3.2）的同工酶模式如何，测定其活性时ADP的最佳试剂浓度选择为2 mmol/L，Mg2+为10 mmol/L，但我们的双变量研究结果使我们建议采用更高的最佳浓度：ADP为4.1至4.7 mmol/L，Mg2+为22 mmol/L。实际上，最大活性区域是一个宽广的平台，以至于在ADP浓度为3至5 mmol/L和Mg2+浓度为17至26 mmol/L时，可达到超过99%的最大酶活性。在这些新条件下，测得的最大活性比先前推荐的方法略有增加（约10%），但预计该测定方法对ADP和Mg2+浓度变化的耐受性更强。可能有必要修改欧洲推荐的方法。
