Luo D, Geng M, Schultes B, Ma J, Xu D Z, Hamza N, Qi W, Noujaim A A, Madiyalakan R
Research and Development, AltaRex Corp., University of Alberta, Edmonton, Canada.
J Biotechnol. 1998 Oct 27;65(2-3):225-8. doi: 10.1016/s0168-1656(98)00094-7.
We constructed two fusion proteins of scFv linked to biotin mimetic sequence (BMS) via different linkers, and expressed them in the Pichia pastoris expression/secretion system. We found that both bi-functional scFv proteins exhibited their intrinsic binding activities to antigen CA125 determined in competitive radioimmunoassay experiments, but the fusion protein with a spacer between the scFv and BMS (scFv-spacer-BMS) showed higher binding activity of streptavidin than the one with c-Myc peptide as a linker.
我们构建了两种通过不同接头连接生物素模拟序列（BMS）的单链抗体片段（scFv）融合蛋白，并在毕赤酵母表达/分泌系统中进行表达。我们发现，在竞争性放射免疫分析实验中测定的这两种双功能scFv蛋白均表现出对抗原CA125的固有结合活性，但在scFv和BMS之间带有间隔序列的融合蛋白（scFv-间隔序列-BMS）显示出比以c-Myc肽作为接头的融合蛋白更高的链霉亲和素结合活性。
