Moriwaki Y, Yamamoto T, Yamakita J, Takahashi S, Tsutsumi Z, Higashino K
Third Department of Internal Medicine, Hyogo College of Medicine Mukogawa-cho 1-1, Japan.
Adv Exp Med Biol. 1998;431:47-50. doi: 10.1007/978-1-4615-5381-6_9.
We describe an enzymatic histochemical localization of two allopurinol-oxidizing enzymes, xanthine oxidase and aldehyde oxidase in rat hepatic tissues. This method is based on the tetrazolium salt procedures by use of a tissue protectant, polyvinyl alcohol, with tetra-nitro BT as the final electron acceptor. The present study demonstrated that both oxidases are present in the cytoplasm of hepatic cells. However, the distribution of the enzymes was uneven, being seen mainly in the pericentral rather than the periportal area. When allopurinol was used as a substrate, the specific staining by xanthine oxidase was more prominent than that of aldehyde oxidase. The results suggested that xanthine oxidase is more effective in oxidizing allopurinol than aldehyde oxidase.
我们描述了大鼠肝组织中两种别嘌呤醇氧化酶（黄嘌呤氧化酶和醛氧化酶）的酶组织化学定位。该方法基于四唑盐程序，使用组织保护剂聚乙烯醇，并以四硝基蓝四唑作为最终电子受体。本研究表明，两种氧化酶均存在于肝细胞的细胞质中。然而，酶的分布并不均匀，主要见于中央静脉周围区域而非门静脉周围区域。当使用别嘌呤醇作为底物时，黄嘌呤氧化酶的特异性染色比醛氧化酶更为明显。结果表明，黄嘌呤氧化酶在氧化别嘌呤醇方面比醛氧化酶更有效。
