Hofman M, Shaffar M
Clin Chem. 1985 Sep;31(9):1478-80.
We have developed a new method for quantifying alpha-amylase (EC 3.2.1.1) in serum and urine by fluorescence depolarization. Amylase in the sample catalyzes the hydrolysis of the substrate, a fluorescein-labeled amylose. This results in decreased fluorescence polarization, owing to the increased rate of rotation of the amylose fragment relative to the intact substrate. The TDx amylase assay is calibrated with six human-serum-based pancreatic amylase calibrators. Amylase activities are determined by interpolation from the calibration curve, which is stored in the TDx analyzer's memory. Results correlate well with those by the Du Pont aca assay and the Beckman "DRI-STAT" assay. Endogenous glucose does not interfere. CVs are less than 6%, and the reagents are stable in liquid form.
我们开发了一种通过荧光偏振定量测定血清和尿液中α淀粉酶（EC 3.2.1.1）的新方法。样品中的淀粉酶催化底物（一种荧光素标记的直链淀粉）的水解。由于直链淀粉片段相对于完整底物的旋转速率增加，这导致荧光偏振降低。TDx淀粉酶测定法使用六种基于人血清的胰腺淀粉酶校准品进行校准。淀粉酶活性通过在校准曲线上插值来确定，校准曲线存储在TDx分析仪的内存中。结果与杜邦aca测定法和贝克曼“DRI - STAT”测定法的结果相关性良好。内源性葡萄糖不产生干扰。变异系数小于6%，并且试剂以液体形式稳定。
