Kream B E, Sauer L A
Endocrinology. 1977 Oct;101(4):1318-24. doi: 10.1210/endo-101-4-1318.
Rat adrenal cortex contains a protein(s) that binds pregnenolone with high affinity. This binding, demonstrated by gel filtration and by a dextran-coated charcoal method, was associated with the cytosol and with fractions solubilized by sonication from the mitochondria and microsomes. The binding of pregnenolone was saturable and was inhibited by mercurials and proteolytic enzymes. Pregnenolone-binding was not influenced by the presence of progesterone, deoxycorticosterone, corticosterone or aldosterone, but was inhibited by steroids with a 3beta-hydroxy-5-ene structure similar to pregnenolone, and by hydroxymethylene steroid and cyanoketone. We suggest that this protein is involved in the intracellular transport and retention of pregnenolone within adrenal cortical cells.
大鼠肾上腺皮质含有一种能与孕烯醇酮高亲和力结合的蛋白质。这种结合通过凝胶过滤和葡聚糖包被活性炭法得以证明,它与胞质溶胶以及通过超声处理从线粒体和微粒体中溶解的组分有关。孕烯醇酮的结合是可饱和的,并受到汞剂和蛋白水解酶的抑制。孕烯醇酮的结合不受孕酮、脱氧皮质酮、皮质酮或醛固酮的影响,但受到具有与孕烯醇酮相似的3β-羟基-5-烯结构的类固醇、羟亚甲基类固醇和氰基酮的抑制。我们认为这种蛋白质参与了肾上腺皮质细胞内孕烯醇酮的细胞内转运和保留。