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Two-step affinity-chromatographic purification of cathepsin D from pig myometrium with high yield

机译:具有高产的两步亲和力 - 色谱纯度从猪肌瘤纯化

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pCathepsin D was purified by two-step affinity chromatography on concanavalin A- and pepstatin-Sepharose. The main purification was achieved by washing the enzyme bound to the pepstatin-Sepharose column with buffered 6 M-urea. This step separated cathepsin D from all low- and high-molecular-weight impurities. Although the 1700-fold purified acid proteinase was homogeneous on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, it still showed microheterogeneity./p
机译:通过两步亲和力色谱法在Concanavalin A-和胃蛋白酶 - Sepharose上纯化组织蛋白酶D.通过用缓冲的6m-urea洗涤与胃抑素 - 琼脂糖柱结合的酶来实现主要纯化。该步骤从所有低分子量和高分子量杂质中分离了组织蛋白酶D.虽然1700倍纯化的酸蛋白酶在十二烷基硫酸钠/聚丙烯酰胺 - 凝胶电泳上均匀,但它仍然显示出微渗透性。

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