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为了获得大量可溶性人类白细胞抗原F(Human leukocyte antigen F,HLA-F)和分化簇8α同二聚体(Cluster of differentiation 8αhomodimers,CD8αα)蛋白并对它们的相互关系进行研究,通过同义突变的方法改变了HLA-F和CD8αα基因序列N端的大肠杆菌稀有密码子,获得了高效表达的HLA-F和CD8αα包涵体蛋白;所表达的蛋白通过稀释法复性后,分别进行了凝胶过滤层析和离子交换纯化。经凝胶过滤层析和native-PAGE检测,推测HLA-F与CD8αα间具有相互作用。该相互作用可能影响其他MHC分子与CD8αα结合,从而调节免疫反应。研究结果对了解和进一步深入研究HLA-F的功能提供了线索。
In order to obtain a large number of human leukocyte antigen F (HLA-F) and cluster of differentiation 8α homodimers (CD8αα) proteins and to study their interrelationships, The rare codons of Escherichia coli at the N-terminus of HLA-F and CD8αα gene sequences were changed to obtain the highly expressed HLA-F and CD8αα inclusion protein. The expressed proteins were refolded by dilution method and subjected to gel filtration chromatography And ion exchange purification. By gel filtration chromatography and native-PAGE detection, it is speculated that HLA-F interacts with CD8αα. This interaction may affect the binding of other MHC molecules to CD8αα, thereby modulating the immune response. The results provide clues for understanding and further studying the function of HLA-F.