Heinz F, Reckel S, Kalden J R
Enzyme. 1979;24(4):247-54. doi: 10.1159/000458666.
A new method for the determination of guanase is described. Xanthine, the product of the guanase reaction, is oxidized by xanthine oxidase, forming uric acid and hydrogen peroxide. Hydrogen peroxide is further reduced to water by catalase in the presence of ethanol. The acetaldehyde formed in this reaction step is dehydrogenated NAD or NADP dependent by aldehyde dehydrogenase. The NADH or NADPH production is measured and utilized for the calculation of the guanase activity. The sensitivity of the method can be doubled by the addition of uricase, which oxidizes uric acid to permit the formation of another mole of hydrogen peroxide.
本文描述了一种测定鸟嘌呤酶的新方法。鸟嘌呤酶反应的产物黄嘌呤被黄嘌呤氧化酶氧化，生成尿酸和过氧化氢。在乙醇存在下，过氧化氢被过氧化氢酶进一步还原为水。该反应步骤中形成的乙醛被醛脱氢酶依赖NAD或NADP脱氢。测量NADH或NADPH的产生并用于计算鸟嘌呤酶活性。通过添加尿酸酶可使该方法的灵敏度提高一倍，尿酸酶将尿酸氧化以允许形成另一摩尔过氧化氢。
