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目的：在大肠杆菌中表达牙本质涎磷蛋白，并对重组蛋白进行纯化，为进一步制备抗牙本质涎磷蛋白抗体和功能研究奠定基础。方法：构建ＤＳＰＰ－ ｐＰｒｏＥＸＨＴｃ 表达载体，重组子以大肠杆菌ＢＬ２１ 为宿主细胞进行诱导表达，表达产物经镍－ 次氮基三乙酸（Ｎｉ－ ＮＴＡ）柱进行亲和层析纯化。结果：工程菌经２０ｈ 诱导后，在ＳＤＳ－ ＰＡＧＥ上出现一条新的蛋白带，Ｍｒ１０７ ×１０３ 左右，经Ｎｉ－ ＮＴＡ 柱纯化后获得纯度为９５ ％ 的小鼠牙本质涎磷蛋白。结论：获得Ｍｒ １０７×１０３ 的牙本质涎磷蛋白。
OBJECTIVE: To express dentin sialophosphoprotein in Escherichia coli and purify the recombinant protein, so as to lay the foundation for the further study on the anti-dentin sialoprotein antibody and its function. Methods: The DSPP-pProEXHTc expression vector was constructed. The recombinant plasmid was induced by E. coli BL21. The recombinant protein was purified by affinity chromatography on Ni-NTA column. Results: After induced by engineering bacteria for 20h, a new protein band appeared on SDS-PAGE, Mr107 × 103. After purified by Ni-NTA column, the purity of mouse dentin sialophosphoprotein was 95%. Conclusion: Dentin sialophosphoprotein Mr 107 × 103 was obtained.