Dikov A, Alexandrov I, Russinova A, Boyadjieva-Michailova A
Institut für Zellbiologie und Morphologie, Bulgarischen Akademie der Wissenschaften, Sofia.
Acta Histochem. 1988;83(1):107-15.
Xanthine oxidase is a flavoprotein which directly catalyses the oxidation of xanthine and hypoxanthine by oxygen or by potassium ferricyanide as an artificial acceptor of protons. In doing so, the potassium ferricyanide is reduced into potassium ferrocyanide which in the presence of manganese(II)ions leads to the manganese(II)ferrocyanide which is insoluble in water and in organic solvents. The latter is deposited on the areas with enzyme activity and marks them under the electron microscope. After the detection of the xanthine oxidase in rat liver on ultrathin non-contrasted sections, it was observed that the fine granular reaction product was deposited only on the peroxisomes of the hepatocytes. A greater quantity of the reaction product is deposited on the outer membrane and the matrix and a smaller one on the nucleoid of these cell organelles. No deposition of the reaction product was observed on the other cell structures. The method can be used for the study of purine metabolism on the cellular level as well as for the specific ultracytochemical detection of the peroxisomes.
黄嘌呤氧化酶是一种黄素蛋白，它可直接催化黄嘌呤和次黄嘌呤被氧气或作为人工质子受体的铁氰化钾氧化。在此过程中，铁氰化钾被还原为亚铁氰化钾，在锰（II）离子存在的情况下，会生成不溶于水和有机溶剂的亚铁氰化锰（II）。后者沉积在具有酶活性的区域，并在电子显微镜下对其进行标记。在超薄非反差切片上检测大鼠肝脏中的黄嘌呤氧化酶后，观察到细颗粒状反应产物仅沉积在肝细胞的过氧化物酶体上。大量反应产物沉积在外膜和基质上，少量沉积在这些细胞器的类核上。在其他细胞结构上未观察到反应产物的沉积。该方法可用于细胞水平的嘌呤代谢研究以及过氧化物酶体的特异性超微细胞化学检测。
