摘要
目的:制备和纯化抗肺炎链球菌工程多肽(Ph-SP)。方法:将重组质粒转化入工程菌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。
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-ex- change 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.
出处
《大理学院学报（综合版）》
CAS
2007年第6期18-20,共3页
Journal of Dali University
基金
国家"十五"重大科技专项"创新药物和中药现代化"基金资助项目(32002AA2Z3350)
国家自然科学基金重点项目资助(30430220)
