中文摘要：

以国产交联琼脂糖6FF为基质，分别以环氧氯丙烷（ECH）、1,4-丁二醇二缩水甘油醚（BDGE）为活化剂，偶联谷胱甘肽（GSH）得到两种连接臂长度不同的GSH亲和层析介质，并以两种自制介质对融合蛋白GST-ADAM15进行了纯化。结果表明：GSH—ECH-琼脂糖凝胶和GSH-BDGE-琼脂糖凝胶的配基密度分别达到了30～35μmol／mL和15—18μmol／mL，经两种介质纯化后的GST融合蛋白，纯度均达到95％以上，BDGE活化对目标蛋白的回收率占总蛋白26％，ECH活化为13％。相对而言，由于连接臂长度的不同，BDGE活化的介质纯化效果优于ECH。

英文摘要：

GSH affinity adsorbents were prepared separately by epichlorohydrin （ECH） and 1,4-butanedioldiglycidyl ether （BDGE）, and then coupled with GSH based on the crosslinked agarose particles. The adsorbents were used to purify the recombinant proteins ADAM15 fused to the affinity tag GST. As a result, the GSH ligand density of the agarose which prepared by ECH and BDGE activation reached 30-35μmol/mL and 15- 18gmol/mL, respectively. They both purified the fusion proteins effectively, and the purity of protein reached 95%. But the recovery rate of the crude proteins in total was different, the rate of BDGE activated gel was 26% and the other was 13%. Comparatively, the purification effect of the GSH affinity adsorbents which activated by BDGE was better due to the long arms.