화학공학소재연구정보센터
학회 한국화학공학회
학술대회 2010년 가을 (10/21 ~ 10/22, 대전컨벤션센터)
권호 16권 2호, p.1588
발표분야 생물화공
제목 A Potent Fusion Expression Partner, Stress Responsive Escherichia Coli Protein A, Enhances the Solubility of Aggregation-prone Heterologous Proteins
초록 It has been reported that a population of stress-responsive proteins are significantly upregulated under the stress condition of growing cultures of Escherichia coli BL21(DE3) compared to the non-stress condition. The expression level of a stress-responsive protein called Protein A is significantly increased under the stress condition. When the stress-responsive protein is used as a fusion partner for the expression of recombinant proteins aggregated to inclusion bodies in E.coli cytoplasm, the solubility of the proteins is significantly enhanced, whereas almost all of the proteins are directly expressed in insoluble state.
To demonstrate that the recombinant proteins maintain their native conformation, hG-CSF is chosen as an example among the proteins fused with E.coli Protein A. The spectra of circular dichroism measured with the purified hG-CSF are identical to that of standard hG-CSF. It implies that the synthesized hG-CSF has native conformation. These results indicate that the bacterial stress-responsive protein can be potent fusion expression partner for aggregation-prone heterologous proteins in E. coli cytoplasm.
저자 송종암, 이대성, 이지원
소속 고려대
키워드 Escherichia Coli; Fusion partner
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