Redondo F L
Clin Chem. 1987 May;33(5):689-91.
Methods for determining alpha-amylase isoenzymes by selective inhibition with a wheat-germ protein are practical and easy, and give accurate, precise results. The incomplete specificity of the inhibitory action is not a major drawback but does necessitate mathematical treatment of the data (i.e., enzymic activities measured before and after preincubation with the inhibitor) to ascertain the amount of the different isoamylases. Such an algorithm is quite simple and straightforward, because the isoenzymes can be calculated either arithmetically or geometrically, by using a linear standard curve, empirically obtained, that relates the fraction of activity remaining after inhibition (R/T) to the pancreatic isoenzyme fraction or to the percentage of total alpha-amylase (P/T or 100 X P/T). An alternative method, plotting R/T against the ratio of pancreatic to salivary isoenzyme (P/S), is inconvenient, necessarily yields a nonlinear curve, needlessly complicates the calculations, and has been a persistent source of confusion in many articles dealing with the differentiation of isoamylases.
用小麦胚芽蛋白选择性抑制法测定α-淀粉酶同工酶的方法实用且简便，能给出准确、精确的结果。抑制作用的不完全特异性并非主要缺点，但确实需要对数据进行数学处理（即与抑制剂预温育前后测得的酶活性）以确定不同异淀粉酶的量。这样一种算法相当简单直接，因为同工酶可以通过算术或几何方法计算，使用一条凭经验获得的线性标准曲线，该曲线将抑制后剩余活性分数（R/T）与胰腺同工酶分数或总α-淀粉酶百分比（P/T或100×P/T）相关联。另一种方法是将R/T与胰腺同工酶与唾液同工酶的比率（P/S）作图，这种方法不方便，必然会产生一条非线性曲线，不必要地使计算复杂化，并且在许多处理异淀粉酶分化的文章中一直是困惑的根源。
