弹性蛋白
融合蛋白
体外
无细胞蛋白质合成
体内
氨基酸
蛋白质生物合成
化学
细胞
蛋白质表达
生物化学
细胞生物学
生物
分子生物学
基因
重组DNA
遗传学
作者
Hun-Su Chu,Kyung-Ho Lee,Ji-Eun Park,Dong-Myung Kim,Byung-Gee Kim,Jong-In Won
标识
DOI:10.1016/j.enzmictec.2009.10.003
摘要
Abstract An elastin-like polypeptide (ELP) fusion protein was expressed in a cell-free protein synthesis system, and the expression profile was analyzed quantitatively. By selective addition of specific amino acids constituting ELP molecules, the expression level of the ELP fusion protein was improved by 1.3–1.8 times as high as positive control. This result implies that the expression amount of long repetitive polypeptides, which was dramatically decreased in vivo system, can be compensated to a degree by adding repeatedly consumed amino acids in vitro system. Presented results demonstrate the potential of cell-free protein synthesis for high-throughput study of various repetitive polypeptides.
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