Watanabe T, Suga T, Hayashi H
J Biochem. 1977 Aug;82(2):607-9.
The cores of peroxisomes were purified 670 fold from a rat liver homogenate and the protein in the preparation was examined by sodium dodecyl sulfate(SDS)-polyacrylamide gel electrophoresis. Two bands of protein were detected on 10% polyacrylamide gel, and their molecular weights were calculated to be about 32,000 and 27,000. On treatment of the core fraction with alkali, urate oxidase was solubilized and on 10% polyacrylamide gel this fraction gave a single band of protein with an estimated molecular weight of 32,000. These results suggests that the protein component having a molecular weight of 27,000 is the framework protein of the core of rat liver peroxisomes.
过氧化物酶体核心从大鼠肝脏匀浆中纯化了670倍，并用十二烷基硫酸钠（SDS）-聚丙烯酰胺凝胶电泳检测了制剂中的蛋白质。在10%聚丙烯酰胺凝胶上检测到两条蛋白带，计算其分子量约为32,000和27,000。用碱处理核心部分后，尿酸氧化酶溶解，在10%聚丙烯酰胺凝胶上，该部分呈现出一条估计分子量为32,000的单一蛋白带。这些结果表明，分子量为27,000的蛋白质成分是大鼠肝脏过氧化物酶体核心的骨架蛋白。
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