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参数Z对疏水色谱中胍变蛋白质分子构象变化的表征
引用本文:卫引茂,常晓青,耿信笃. 参数Z对疏水色谱中胍变蛋白质分子构象变化的表征[J]. 分析化学, 1997, 0(9)
作者姓名:卫引茂  常晓青  耿信笃
作者单位:西北大学现代分离科学研究所!现代分离科学陕西省重点实验室,西安710069,西北大学现代分离科学研究所!现代分离科学陕西省重点实验室,西安710069,西北大学现代分离科学研究所!现代分离科学陕西省重点实验室,西安710069
基金项目:国家自然科学基金资助课题。
摘    要:用计量置换参数Z对疏水色谱流动相中存在盐酸胍时蛋白质分子构象变化进行了表征。除溶菌酶外,其余4种蛋白质的Z值随盐酸胍浓度的增大先增大,而后减小。将盐酸胍和脲对蛋白质Z值的影响进行了比较后发现,在疏水色谱中Z值作为蛋白质分子构象变化表征的一个重要的结论是随变性剂浓度的增大,埋藏在蛋白质分子内部的疏水性氨基酸残基暴露到分子表面的程度逐渐增大,造成了Z值随蛋白质分子构象变化程度的增大而减小。蛋白质的Z值随盐酸胍及脲浓度变化的不同特点,反映了两者对蛋白质变性机理的不同。

关 键 词:蛋白质  疏水色谱  计量置换  盐酸胍  分子构象

Characterization of the Relationship Between Concentration of Guanidine Bydrochloride and Molecular Conformation of Biopolymers in Hydrophobic Interaction Chromatography by Parameter Z
Wei Yinmao,Chang Xiaoqing,Geng Xindu. Characterization of the Relationship Between Concentration of Guanidine Bydrochloride and Molecular Conformation of Biopolymers in Hydrophobic Interaction Chromatography by Parameter Z[J]. Chinese Journal of Analytical Chemistry, 1997, 0(9)
Authors:Wei Yinmao  Chang Xiaoqing  Geng Xindu
Abstract:The Z value of the stoichiometric displacement model for retention (SDM-R) was used to characterize the changes in the molecular conformations of proteins. Except lysozyme, the Z values of other four kinds of proteins were found to increase firstly, and then decrease with increasing concentration of guanidine hydrochloride (GuHCl) in the mo- bile phase used. After comparing the effects of various kinds of denaturants, urea, and GuHCl on the Z values of proteins, we found that the hydrophobic amino acid residues buried in the interna1 of protein molecules exposed gradually to the surfaces of the molecules with increasing concentration of the denaturant used. As a result, the Z values of proteins decrease. The different changes in Z values of proteins with the concentration of GuHCl and urea reflect different denaturation mechanisms of proteins induced by these two denaturants.
Keywords:Protein   hydrophobic interaction chromatography   stoichiometric displacement   guanidine hydrochloride   molecular conformation
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