作者: Ronald J. Moore , Jean D. Wilson
DOI: 10.1016/S0021-9258(19)45700-1
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摘要: Abstract The intranuclear localization of the 5α-reductase that converts testosterone to dihydrotestosterone in rat ventral prostate has been investigated nuclei purified by sedimentation through 2.2 m sucrose. First, as result chemical analyses isolated nuclei, light microscopy studies, and an investigation subcellular distribution several marker enzymes this tissue, it was concluded prepared manner were free from major contamination with other cytoplasmic constituents. In keeping previous studies enzyme approximately half activity found nucleus. Second, fragmented exposure sonic oscillation subjected centrifugation previously formed cesium chloride density gradients. Under these conditions, all coincide a visible band turbidity at d 1.23 1.27. On basis buoyant density, composition fraction, similar flotation patterns NADH-cytochrome c reductase, known nuclear membrane, prostatic is located membrane. isolation membrane fraction 90-fold purification achieved.