重组人神经肽Y受体Y1融合蛋白的表达纯化及其生物信息学分析研究临床医学.docVIP

重组人神经肽Y受体Y1融合蛋白的表达纯化及其生物信息学分析研究临床医学 目录 TOC \o 1-9 \h \z \u 目录 1 正文 1 文1：重组人神经肽Y受体Y1融合蛋白的表达纯化及其生物信息学分析研究临床医学 1 1 材料与方法 3 2 结 果 5 3 讨 论 8 文2：重组人神经肽Y受体Y2融合蛋白的表达纯化及其生物信息学分析研究临床医学 9 1 材料与方法 10 2 结 果 13 3 讨 论 15 参考文摘引言： 17 原创性声明（模板） 18 文章致谢（模板） 18 正文 重组人神经肽Y受体Y1融合蛋白的表达纯化及其生物信息学分析研究临床医学 文1：重组人神经肽Y受体Y1融合蛋白的表达纯化及其生物信息学分析研究临床医学 【Abstract】 Objective To express human Y1 receptor protein in E. coli，purify and identify it，and conduct bioinformatic analysis of Y1 receptor protein. Methods The recombinant plasmid pET28aY1 which had been well cotructed and sequentially confirmed was traplanted into (DE3) and induced by IPTG to express fusion protei. SDSPAGE and Western blot were used to test and identify the expressed fusion protei. The inclusion body of the expressed product was purified by Ni2+NTA affinity chromatography. Then bioinformatic analysis of the Y1 receptor was conducted with the help of related online software. Results After being induced by IPTG，the DE3 with recombinant plasmid pET28aY1 expressed recombinant human Y1 receptor protein. Highly purified fusion protein was obtained by Ni2+NTA affinity chromatography. Related biological characteristics of Y1 receptor were obtained after the online software analysis. Conclusio The recombinant plasmid pET28aY1 can be successfully expressed in DE3. Highly purified protei can be obtained by Ni2+NTA affinity chromatography. Y1 receptor′s biological characteristics are predicted, which lay foundation for further studies of Y1 receptor protein′s biological function and antibody development. 【Key words】 NeuropeptideY Y1 receptor; Fusion protein; Inclusion body; Purification; Bioinformatics 神经肽Y(Neuropeptide,NPY)是一种内源性的促食欲因子，NPY主要通过与相应受体结合起作用。其受体(Receptor)主要有Y1、Y2、Y3、Y4、Y5和Y6受体亚型,属于G蛋白偶联的受体家族。这些受体亚型介导信息传导均与G蛋白偶联有关,均能抑制腺苷酸环化酶的生物合成,最终动员或抑制钙离子释放。不同受体起不同的作用,各组织所含受体种类及分布密度也不相同〔1～4〕。NPY Y1、Y2和Y5受体(NPY1R,NPY2R,NPY5R)被认为与NPY诱导摄食和引起肥胖的作用机制有关。实验表明,在NPY1R缺失小鼠中NPY诱导的摄食效应明显减弱〔5〕;肥胖大鼠口服NPY1R抑制剂能够抵抗肥胖