Heinz F, Reckel S, Pilz R, Kalden J R
Enzyme. 1980;25(1):50-5. doi: 10.1159/000459215.
A new spectrophotometric method for the determination of adenosine deaminase is described. Adenosine is deaminated to inosine, the latter is cleaved by an inosine-guanosine specific nucleoside phosphorylase to hypoxanthine and ribose-1-phosphate. Hypoxanthine can be oxidized further to uric acid by xanthine oxidase or to allantoin by xanthine oxidase and uricase. The hydrogen peroxide formed in these reactions is reduced by catalase to water. In the presence of high concentrations of ethanol, equivalent amounts of acetaldehyde are produced. The acetaldehyde is oxidized NAD(P) dependent and the production rate of NAD(P)H is recorded at 334 nm. The new method is suitable for the detection of adenosine deaminase in whole blood, lymphocytes, sera and tissues.
本文描述了一种测定腺苷脱氨酶的新分光光度法。腺苷被脱氨生成肌苷，肌苷被肌苷-鸟苷特异性核苷磷酸化酶裂解为次黄嘌呤和磷酸核糖-1-磷酸。次黄嘌呤可被黄嘌呤氧化酶进一步氧化为尿酸，或被黄嘌呤氧化酶和尿酸酶氧化为尿囊素。这些反应中生成的过氧化氢被过氧化氢酶还原为水。在高浓度乙醇存在下，会产生等量的乙醛。乙醛在依赖NAD(P)的情况下被氧化，并在334nm处记录NAD(P)H的生成速率。该新方法适用于检测全血、淋巴细胞、血清和组织中的腺苷脱氨酶。
