Hüttinger M, Pavelka M, Goldenberg H, Kramar R
Histochemistry. 1981;71(2):259-67. doi: 10.1007/BF00507829.
Membranes of liver peroxisomes from rats fed with clofibrate were purified in a discontinuous gradient using a zonal rotor. The preparation consists of round or oval vesicles mostly devoid of nucleoids with a diameter ranging from 70-700 nm; open sheets are found very infrequently. Mitochondrial profiles as well as vesicles containing cytochemically demonstrable glucose 6-phosphatase are scarce; accordingly, glucose 6-phosphatase is nearly undetectable biochemically. Monoamine oxidase is absent in peroxisomal membranes. Cytochrome b5 is found in a concentration of 0.3 nmoles/mg protein, an order of magnitude comparable to the content of endoplasmic reticulum membranes. Reduction of this cytochrome with palmitoyl-CoA is possible only after recombination of the membranes with the soluble peroxisomal matrix fraction.
用区带转头在不连续梯度中纯化用氯贝丁酯喂养的大鼠肝脏过氧化物酶体膜。制备物由大多不含类核的圆形或椭圆形囊泡组成，直径范围为70 - 700纳米；很少发现开放的片层。线粒体轮廓以及含有可通过细胞化学方法证实的葡萄糖6 -磷酸酶的囊泡很少；因此，葡萄糖6 -磷酸酶在生化上几乎检测不到。过氧化物酶体膜中不存在单胺氧化酶。细胞色素b5的浓度为0.3纳摩尔/毫克蛋白质，与内质网膜的含量相当。只有在膜与可溶性过氧化物酶体基质部分重组后，棕榈酰辅酶A才能使这种细胞色素还原。
