[1]谭兵,张德纯,汪正清.重组人可溶性补体受体1型SCR15-18片段表达纯化及生物活性鉴定[J].陆军军医大学学报(原第三军医大学学报),2007,29(10):892-895.
　TAN Bing,ZHANG De-chun,WANG Zheng-qing.Expression, purification and bioactivity identification of recombinant SCR15-18 domain of human soluble complement receptor type 1[J].J Amry Med Univ (J Third Mil Med Univ),2007,29(10):892-895.
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重组人可溶性补体受体1型SCR15-18片段表达纯化及生物活性鉴定
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陆军军医大学学报（原第三军医大学学报）[ISSN:1000-5404/CN:51-1095/R]

卷:
29卷
期数:
2007年第10期
页码:
892-895
栏目:
论著
出版日期:
2007-05-30

文章信息/Info

Title:
Expression, purification and bioactivity identification of recombinant SCR15-18 domain of human soluble complement receptor type 1
作者:
谭兵;  张德纯;  汪正清
第三军医大学基础医学部微生物学教研室，重庆市微生物工程实验室；重庆医科大学基础医学院病原生物学教研室，临床检验诊断学省部共建教育部重点实验室
Author(s):
TAN Bing;  ZHANG De-chun;  WANG Zheng-qing
Department of Microbiology, College of Medicine, Third Military Medical University, Chongqing 400038, Key Laboratory of Laboratory Medical Diagnostics of Ministry of Education, Chongqing Medical University, Chongqing 400016, China
关键词:
可溶性补体1型受体; 表达; 包含体; 纯化; 复性
Keywords:
soluble complement receptor type 1;  expression;  inclusion body;  purification;  refolding
分类号:
R392-33；R392.11；R392.13
文献标志码:
A
摘要:
目的    获得高表达、高纯度和高活性的可溶性补体受体1型SCR15-18 (sCR1-SCR15-18）蛋白。    方法    重组原核表达载体pET32a-sCR1-SCR15-18 在大肠杆菌BL21中经不同IPTG浓度、诱导时间和温度诱导表达，超声破菌，提取包含体，经Ni2+-NTA 亲和层析后，选择不同氧化还原条件进行复性，进而检测其生物学活性。    结果    得到了有较高表达量、较高纯度和较好生物学活性的sCR1-SCR-15-18蛋白。    结论    优化了sCR1-SCR15-18蛋白的表达、纯化和复性的参数，所获结果为进一步动物体内保护实验研究奠定了基础。
Abstract:
Objective    To prepare highly expressed, purified and refolded SCR15-18 of human soluble complement receptor type 1 (sCR1-SCR15-18) protein.     Methods    The expression of recombinant pET32-sCR1-SCR15-18 in E.coli.. BL21 was induced by IPTG of different concentrations for different time period under different temperatures and the bacteria were split by sonication. The sCR1-SCR15-18 protein was purified by Ni2+-NTA resin affinity chromatography. The purified protein was refolded under different conditions. Then the bioactivity of the protein was analyzed.     Results    The sCR1-SCR15-18 protein of high expression, purity and bioactivity was attained.     Conclusion    The parameters of expression, purification and refolding of sCR1-SCR15-18 protein were optimized, which may pave a way for further studies.

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更新日期/Last Update: 2008-10-24