L-精氨酸对提高蛋白质复性与纯化率的作用及其分析  

Effect and Analysis of the Addition of L-arginine in the Renaturation and Purification Process of Denatured Protein

作　　者：余秀娟 王骊丽[3] 张如月[1] 高一笑 YU Xiu-juan;WANG Li-li;ZHANG Ru-yue;GAO Yi-xiao(School of Chemistry and Chemical Engineering Inner Mongolia University, Hohhot 010021, China;Department of Pharmacy, Hebei North University ,Zhangjiakou 075000,China;Institute of Modern Separation Science, Northwest University ,Key Laboratory of Synthetic and Natural Functional Molecular Chemistry of Ministry of Education, Shanxi Key Laboratory of Modern Separation Science, Xi＇ an 710069, China)

机构地区：[1]内蒙古大学化学化工学院,呼和浩特010021 [2]河北北方学院药学系,河北张家口075000 [3]西北大学现代分离科学研究所,合成及天然功能性分子化学教育部重点实验室,陕西省分离科学重点实验室,西安710069

出　　处：《内蒙古大学学报（自然科学版）》2017年第6期612-618,共7页Journal of Inner Mongolia University：Natural Science Edition

基　　金：张家口市科学技术和地震局项目(1521001A);河北北方学院青年课题项目(Q2014022)

摘　　要：分别以还原变性的溶菌酶(Lys)和大肠杆菌(Escherichia coli)中表达的重组人酪氨酸激酶配体(Recombined human Flt3ligand,rhFL)为不同来源的变性蛋白,利用荧光光谱技术分析L-精氨酸(L-arginine,L-Arg)作为小分子添加剂时,蛋白质折叠液相色谱(PFLC)法对变性蛋白质的复性效果,以及变性蛋白复性过程中的复性效率、荧光强度与蛋白构象变化的规律与关系,为解决包涵体蛋白质难于复性和复性效率低的问题提供可靠的数据.The denatured lysozyme（Lys）and the recombined human Flt3 ligand（rhFL）which express in Escherichia coli are different sources for denatured protein.The L-arginine as a small molecular additive in liquid chromatography for protein folding（PFLC）is used to analyze the result of refolding denatured protein by fluorescence spectroscopy technology.The analysis includes the relationship of the renaturation efficiency,the fluorescence intensity and the change of protein conformation in the denatured protein folding process.The results provide reliable data for solving the difficulties in refolding proteins from inclusion bodies and their low refolding efficiency.

关 键 词：L-精氨酸 荧光光谱 蛋白质折叠液相色谱法 蛋白质复性 

分 类 号：O657.72[理学—分析化学]