Heinz F, Reckel S, Kalden J R
Enzyme. 1979;24(4):239-46. doi: 10.1159/000458665.
A new method for the determination of xanthine oxidase activity with xanthine or hypoxanthine is described. The hydrogen peroxide produced by the oxidation of the substrates is reduced by catalase in the presence of high concentrations of ethanol. The acetaldehyde formed is further oxidized by aldehyde dehydrogenase NAD or NADP-dependent. The reduction rate of the coenzymes were measured at 334 nm and utilized as indicators for the xanthine oxidase. The sensitivity of the method with xanthine as substrate can be doubled by the addition of uricase, which oxidizes uric acid to allantoin.
描述了一种用黄嘌呤或次黄嘌呤测定黄嘌呤氧化酶活性的新方法。在高浓度乙醇存在下，底物氧化产生的过氧化氢被过氧化氢酶还原。形成的乙醛被依赖NAD或NADP的醛脱氢酶进一步氧化。在334nm处测量辅酶的还原速率，并将其用作黄嘌呤氧化酶的指标。以黄嘌呤为底物的方法通过添加尿酸酶可使灵敏度提高一倍，尿酸酶将尿酸氧化为尿囊素。
