CAJ | 학술논문

为获得目标蛋白以用于蛋白功能解析，本研究将锌指蛋白C2H2以GST（Glutathion eS-transferase）融合蛋白的形式进行了表达，并确定了表达的最佳条件：37℃、IPTG诱导4h、IPTG终浓度为1．0mmol／L。利用固定化的还原型谷胱甘肽（GSH）对GST-C2H2融合蛋白进行一步亲和纯化，获得目标融合蛋白，25倍超滤浓缩之后测定其浓度为1．762mg／mL。
위획득목표단백이용우단백공능해석，본연구장자지단백C2H2이GST（Glutathion eS-transferase）융합단백적형식진행료표체，병학정료표체적최가조건：37℃、IPTG유도4h、IPTG종농도위1．0mmol／L。이용고정화적환원형곡광감태（GSH）대GST-C2H2융합단백진행일보친화순화，획득목표융합단백，25배초려농축지후측정기농도위1．762mg／mL。
In order to obtain target protein for protein fimction analysis, this study expressed the zinc finger protein C2H2 with GST （Glutathione S-transferase） fusion protein and determined the best condition of the fusion protein expression： 37℃, induced by IPTG for 4 hours and the IPTG final concentration was 1.0 mM. Using immobilized and reduced glutathione （GSH） purified the GST-C2H2 fusion protein, target fusion protein could be obtained. The concentration of the GST-C2H2 fusion protein is 1.762 mg/ml after 25 times concentrated by ultrafiltration.