【摘要】 本文报道利用阳离子交换层析,纯化了雄激素依赖的大鼠储精囊分泌蛋白(SVPⅡ、SVPⅣ、SVPⅤ_a、SVPⅤ_b及SVPⅥ)。主要纯化步骤包括下列二步:1.Sep-hadex G-100凝胶过滤;2.上样后,联合使用盐梯度和pH梯度,洗脱快速蛋白液相层析(FPLC)系统的阳离子交换柱Mono S。洗脱峰的纯度以变性条件下的聚丙烯酰胶凝胶电泳(SDS-PAGE)和等电聚焦(IEF)鉴定;借此,还测定了已纯化的大鼠储精囊分泌蛋白的分子量和等电点。更多还原

【Abstract】 The major androgen-regulated secretory proteins of rat seminal vesicles (SVPⅡ. SVPⅣ. SVPⅤa. SVPb. SVPⅥ) have been purified by high-performance cation-exchange chromatography. The purification procedure involved two steps: 1. gel chromatography on Seph adex G-100 and 2. cation exchange on Mono S column in FPLC system by using combined salt and pH gradients. The purity of selected peaks was evaluated by sodium dodecyl sulphate polyacrylamide gel electrophoresis and isoelectric focusing. The molecular weight and pi of purified SVP were determined by using SDS-PAGE and IEF.更多还原