Sano T, Cantor C R
Department of Molecular and Cell Biology, University of California, Berkeley.
Biotechnology (N Y). 1991 Dec;9(12):1378-81. doi: 10.1038/nbt1291-1378.
We have expressed a gene fusion of streptavidin and the two immunoglobulin G (IgG)-binding domains of protein A in Escherichia coli. The purified chimeric protein had full biotin-binding ability, and bound one IgG molecule per subunit (31.4 kD). The affinity of the chimeric protein both for biotin and IgG can be used to provide antibody molecules with additional recognition capabilities. For example, the chimera will allow any IgG molecule to be used for sensitive biotin-linked detection systems without the need for chemical modification.
我们在大肠杆菌中表达了链霉亲和素与蛋白A的两个免疫球蛋白G(IgG)结合结构域的基因融合体。纯化后的嵌合蛋白具有完整的生物素结合能力,每个亚基(31.4 kD)可结合一个IgG分子。嵌合蛋白对生物素和IgG的亲和力可用于赋予抗体分子额外的识别能力。例如,该嵌合体将使任何IgG分子都可用于灵敏的生物素连接检测系统,而无需进行化学修饰。