Brégégère F, Bedouelle H
Unité de Biochimie cellulaire, C.N.R.S.-U.A. n. 1129, Institut Pasteur, Paris.
C R Acad Sci III. 1992;314(12):527-32.
We have fused the variable domains of a mouse antibody to the C-terminal end of the maltose-binding protein (malE), at the genetic level. The hybrid proteins were expressed in E. coli under control of the malEp promoter, and exported to the periplasm, at low temperature. They were purified by affinity chromatography on cross-linked amylose. When the two variable domains were fused together through a peptide link, the hybrid displayed similar affinity and specificity to the antigen as the native antibody.
我们在基因水平上，将小鼠抗体的可变结构域融合到麦芽糖结合蛋白（malE）的C末端。这些杂合蛋白在malEp启动子的控制下于大肠杆菌中表达，并在低温下输出到周质空间。它们通过交联直链淀粉亲和层析进行纯化。当两个可变结构域通过肽连接融合在一起时，该杂合体对抗原显示出与天然抗体相似的亲和力和特异性。
