Satomura S, Okajima S, Hamanaka T, Shintani A, Miyashita Y, Sakata Y
Clin Chim Acta. 1984 Mar 27;138(1):21-9. doi: 10.1016/0009-8981(84)90350-4.
The enzymatic measurement of alpha-amylase in human serum with chemically modified amylose as substrate was studied. Several substitutions of carboxymethylamylose were prepared from amylose, suitable amounts of monochloroacetic acid, and sodium hydroxide. The relationship between the degree of substitution of the carboxymethylamylose and the kinetic parameters of human pancreatic, salivary and porcine pancreatic alpha-amylases was determined. The action of alpha-amylases on such modified amyloses in the presence of glucoamylase was measured by a specific enzymatic assay having glucose as the product. The kinetic parameters of human pancreatic alpha-amylase were similar to those of human salivary alpha-amylase. It was possible to determine suitable sensitivities for the alpha-amylase assay using this substrate. These results suggested a subsite model.
研究了以化学修饰的直链淀粉为底物酶法测定人血清中α-淀粉酶的方法。由直链淀粉、适量的一氯乙酸和氢氧化钠制备了几种羧甲基直链淀粉取代物。测定了羧甲基直链淀粉的取代度与人胰腺、唾液和猪胰腺α-淀粉酶动力学参数之间的关系。在存在葡糖淀粉酶的情况下，通过以葡萄糖为产物的特异性酶法测定α-淀粉酶对这种修饰直链淀粉的作用。人胰腺α-淀粉酶的动力学参数与人唾液α-淀粉酶的相似。使用该底物有可能确定α-淀粉酶测定的合适灵敏度。这些结果提示了一个亚位点模型。
