Enosawa S, Ohashi A
Biochem Biophys Res Commun. 1986 Dec 30;141(3):1145-50. doi: 10.1016/s0006-291x(86)80163-2.
Fractionation of yeast mitochondria by controlled hypotonic treatment revealed that the enzyme for heme attachment to apocytochrome c was localized in mitochondrial inner membrane. Trypsin digestion of mitoplasts resulted in a considerable loss of enzymatic activity, whereas the enzyme in intact mitochondria resisted the digestion. Triton X-100 solubilized the enzyme from the membrane but high concentration of salt did not. These results reveal that the enzyme for heme attachment is localized in mitochondrial inner membrane facing the cytoplasmic surface.
通过控制性低渗处理对酵母线粒体进行分级分离,结果表明,血红素与脱辅基细胞色素c结合的酶定位于线粒体内膜。胰蛋白酶对线粒体球状体的消化导致酶活性大幅丧失,而完整线粒体中的酶则能抵抗这种消化。Triton X-100可使该酶从膜上溶解下来,但高浓度盐则不能。这些结果表明,血红素结合酶定位于线粒体内膜面向细胞质的表面。