利用外膜蛋白C作为锚定基序在大肠杆菌细胞表面展示多组氨酸肽。
Display of polyhistidine peptides on the Escherichia coli cell surface by using outer membrane protein C as an anchoring motif.
作者信息
Xu Z, Lee S Y
机构信息
Department of Chemical Engineering and BioProcess Engineering Research Center, Korea Advanced Institute of Science and Technology, Yusong-gu, Taejon 305-701, Korea.
出版信息
Appl Environ Microbiol. 1999 Nov;65(11):5142-7. doi: 10.1128/AEM.65.11.5142-5147.1999.
Abstract
A novel cell surface display system was developed by employing Escherichia coli outer membrane protein C (OmpC) as an anchoring motif. Polyhistidine peptides consisting of up to 162 amino acids could be successfully displayed on the seventh exposed loop of OmpC. Recombinant cells displaying polyhistidine could adsorb up to 32.0 micromol of Cd(2+) per g (dry weight) of cells.
摘要
通过利用大肠杆菌外膜蛋白C（OmpC）作为锚定基序，开发了一种新型细胞表面展示系统。由多达162个氨基酸组成的多组氨酸肽可以成功地展示在OmpC的第七个暴露环上。展示多组氨酸的重组细胞每克（干重）细胞最多可吸附32.0微摩尔的Cd(2+)。
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