通过对贻贝珍珠质蛋白EFP分析,发现该蛋白的重要保守域C1Q值得进一步研究.在不以贻贝为材料的前提下,设计引物以基因扩增的方式合成了该基因.经过蛋白的表达纯化与复性,首次使用大肠杆菌制备了可溶的C1Q蛋白.该蛋白具有预期的二级结构与金属离子结合活性,为进一步研究打下了基础.
Analysis of Mytilus edulis nacre protein EFP found C1 Qto be a conserved domain.Suitable primers were designed to synthesize the target gene by polymerase chain reaction,instead of using traditional approaches with mussel materials.After purification and refolding,soluble C1 Q was obtained from a bacterial expression system.The refolded C1 Qexhibited anticipated secondary structure and metal ion binding ability,making the C1 Qpreparation suitable for further study.