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抗肺炎链球菌工程多肽的制备研究
引用本文:秦燕,孙亮,戴萍,张杰,丘小庆.抗肺炎链球菌工程多肽的制备研究[J].大理学院学报,2007,6(6):18-20.
作者姓名:秦燕  孙亮  戴萍  张杰  丘小庆
作者单位:1. 大理学院基础医学院生理学与病理生理学教研室,云南大理,671000
2. 四川大学华西医院卫生部移植工程与移植免疫重点实验室,四川成都,610041
基金项目:国家科技专项基金 , 国家自然科学基金
摘    要:目的:制备和纯化抗肺炎链球茵工程多肽(Ph-SP).方法:将重组质粒转化入工程茵TGl表达工程多肽,经透析、离子交换柱纯化后,SDS-PAGE凝胶电泳鉴定融合蛋白,微平板法测定蛋白浓度.结果:经透析、离子交换柱纯化后可获得较为单一的目的蛋白,蛋白浓度为0.18mg/ml.结论:本文的操作流程可以获得相对单一的目的蛋白.

关 键 词:抗肺炎链球菌工程多肽  制备  纯化
文章编号:1672-2345(2007)06-0018-03
修稿时间:2007-01-07

Study on preparation of Pheromonicin-SP
QIN Yan,SUN Liang,DAI Ping,ZHANG Jie,QIU Xiao-qing.Study on preparation of Pheromonicin-SP[J].Journal of Dali University,2007,6(6):18-20.
Authors:QIN Yan  SUN Liang  DAI Ping  ZHANG Jie  QIU Xiao-qing
Institution:1. Physiology and Pathophysiology Department of School of Basic Medicine, Dali University, Dali, Yunnan 671000, China; 2. Laboratory of Transplant Engineering and Immunology, West China Hospital, Sichuan University, Chengdu, Sichuan 610041, China
Abstract:Objective: To prepare and purify Ph-SP.Methods: The encoding plasmid was transformed into E.coli TG1 cells to produce the fusion peptide,Pheromonicin-Streptococcus pneumoniae(Ph-SP),the peptide was purified by CM sepharose ion-exchange column,and fusion peptide was identified with SDS-PAGE and the concentration of peptide was measured with mini-plate process.Result: The single fusion peptide can be obtained via dialysis and purification by CM sepharose ion-exchange column with concentration of 0.18mg/ml Conclusion: Single fusion peptide can be obtained via this protocols.
Keywords:Pheromonicin-SP  preparation  purification
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