Fusion protein expression was induced by IPTG. After renaturation, the protein was purified by affinity chromatography and the bioactivity was examined by ELISA.
IPTG诱导表达融合蛋白，包涵体蛋白经复性后亲和层析法纯化，ELISA方法测定蛋白活性。
After dissolution of inclusion bodies in binding buffer containing 8m Urea, the fusion protein was purified with metal affinity chromatography column, high purity protein was achieved.
包涵体蛋白经含8m尿素的结合缓冲液溶解后，用金属亲和层析法进行纯化，获得了高纯度的目的蛋白。
The GST-MBD4 fusion protein was purified from cell lysates using glutathione Sepharose 4b affinity chromatography.
用谷胱甘肽琼脂糖凝胶4b亲和介质从菌体裂解液中纯化了GST -MBD4融合蛋白。
The GST-MBD4 fusion protein was purified from cell lysates using glutathione Sepharose 4b affinity chromatography.
用谷胱甘肽琼脂糖凝胶4b亲和介质从菌体裂解液中纯化了GST -MBD4融合蛋白。
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