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大炎肽在胰腺中相互作用蛋白的纯化鉴定
Isolation and characterization of a binding protein of daintain in pancreas
【摘要】 为研究大炎肽影响胰腺β细胞的机制,将大炎肽偶联到CNBr活化的Sepharose 4B亲和层析介质上,利用亲和纯化的方法垂钓其在胰腺组织中的相互作用蛋白,并对纯化蛋白进行胰蛋白酶水解,测定水解片段的分子质量和其中2个片段的氨基酸序列,在MASCOT数据库中检索,鉴定此蛋白为胱硫醚β-合成酶,结果提示大炎肽可能通过结合胱硫醚β-合成酶,调节其活性,造成同型半胱氨酸积累。
【Abstract】 Daintain,a macrophage inflammatory factor,was characterized.To investigate the regulatory mechanism of daintain on pancreatic β cells,daintain was coupled to CNBr-Sepharose 4B,and the binding protein of daintain in pancreas was isolated by affinity chromatography,then it was characterized as cyatathionine-beta-synthase(CBS) in the database of mascot according to the peptide mass fingerprint and amino acid sequence of two peptide fragments with trpsin digestion.The interaction of daintain with CBS suggests that daintain may regulate the activity of CBS,resulting in the accumulation of homocysteine.
【Key words】 daintain; cyatathionine-beta-synthase(CBS); binding protein; homocysteine; pancreas; trypsin; peptide mass fingerprint;
- 【文献出处】 华中农业大学学报 ,Journal of Huazhong Agricultural University , 编辑部邮箱 ,2011年05期
- 【分类号】R363
- 【被引频次】1
- 【下载频次】73