您的位置：首页 > 论文页面
镍离子金属螯合亲和层析纯化重组类人胶原蛋白
发表时间：2013-03-15 浏览量：1562 下载量：393
| 全部作者： | 乔媛媛，范代娣，邓建军，惠俊峰，朱晨辉，马晓轩 |
| 作者单位： | 西北大学化工学院；西北工业大学，陕西省可降解生物医用材料重点实验室 |
| 摘 要： | 以Ni2+快流速琼脂糖凝胶为层析介质，分别采用咪唑洗脱和降低pH值洗脱方式对重组类人胶原蛋白(recombinant human-like collagen，RHLC)进行纯化，收集洗脱部分，SDS-PAGE检测蛋白纯度。结果表明：以含20 mmol/L NaH2PO4, 0.5 mol/L NaCl（pH= 4.0）的洗脱缓冲液进行降低pH值洗脱所得蛋白纯度和收率最好，所得蛋白纯度达99%以上，回收率为76%. 纯化的RHLC为电泳纯，分子量为97 ku. |
| 关 键 词： | 蛋白质工程；金属螯合亲和层析；类人胶原蛋白；纯化 |
| Title： | Purification of recombinant human-like collagen by Ni(II)-based immobilized metal ion affinity chromatography |
| Author： | QIAO Yuanyuan, FAN Daidi, DENG Jianjun, HUI Junfeng, ZHU Chenhui, MA Xiaoxuan |
| Organization： | College of Chemical Engineering, Northwest University; Shaanxi Key Laboratory of Degradable Biomedical Materials, Northwest Unirersity |
| Abstract： | In this paper, the recombinant human-like collagen (RHLC) was purified by elution methods of iminazole and lower pH respectively with Ni2+ sepharose fast flow as the affinity medium. Various fractions of elution were collected and then protein purity was identified for by SDS-PAGE. The results showed that the purity and the recovery of the RHLC is the best by the lower pH elution with the buffer (20 mmol/L NaH2PO4, 0.5 mol/L NaCl, pH=4.0). The protein purity was more than 99%, and the recovery rate was 76%. The purified RHLC was electrophoretically pure with a relative molecular weight of 97 ku. |
| Key words： | protein engineering; immobilized metal ion affinity chromatography; recombinant human-like collagen; purification |
| 发表期数： | 2013年3月第5期 |
| 引用格式： | 乔媛媛，范代娣，邓建军，等. 镍离子金属螯合亲和层析纯化重组类人胶原蛋白[J]. 中国科技论文在线精品论文，2013，6（5）：402-406. |
0
评论数 0请您登录
暂无评论
下载全文
多维论文