首页 | 本学科首页   官方微博 | 高级检索  
     检索      

pH诱导牛血清白蛋白芳香氨基酸残基微环境变化的光谱分析
引用本文:魏晓芳,丁西明,刘会洲.pH诱导牛血清白蛋白芳香氨基酸残基微环境变化的光谱分析[J].光谱学与光谱分析,2000,20(4):556-559.
作者姓名:魏晓芳  丁西明  刘会洲
作者单位:1. 中国科学院化工冶金研究所分离科学与工程青年实验室,100080,北京
2. 中国科学院感光化学研究所,100021,北京
基金项目:中科院“九五”项目资助,国家自然科学重点基金
摘    要:用荧光光谱和紫外吸收光谱研究了pH=2.3~11.3范围内牛血清白蛋白(BSA)芳香氨基酸残基微环境的变化,以此推断蛋白质构象的变化,并讨论蛋白质表面疏水性变化的趋热。与中性环境相比,pH为2.3时,色氨酸微环境的疏水性增强,蛋白质局部表面疏水降低;pH为11.3时,部分Phe残基微环境的极性增强,表明碱诱导蛋白质分子变性使蛋白质分子充分伸展,将更多疏水性氨基酸残基暴露于溶剂中。

关 键 词:牛血清白蛋白  构象  表面疏水性  光谱分析

Spectral Study of the Microenviroment Change of Aromatic Amino-acid Residues in BSA Induced by pH
Xiaofang WEI,Ximing DING,Huizhou LIU.Spectral Study of the Microenviroment Change of Aromatic Amino-acid Residues in BSA Induced by pH[J].Spectroscopy and Spectral Analysis,2000,20(4):556-559.
Authors:Xiaofang WEI  Ximing DING  Huizhou LIU
Institution:Young Scientist Laboratory of Separation Science and Engineering, Institute of Chemical Metallurgy, Chinese Academy of Sciences, 100080 Beijing.
Abstract:The microenvironment change of aromatic amino acid residues in BSA at various pH were studied by fluorescence spectra and ultraviolet absorption spectra.It suggested that the change of protein surface and surface hydrophobicity from result.Compared to neutral pH,the Trp microenvironment seemed to be more hydrophobic at lower pH indicating less local surface hydrophobicity of BSA.At higher pH,the protein undergo conformational changes and undold,the more buried Phe exposed to solvents consistent with stronger surface hydrophobicity of BSA.
Keywords:Bovine serum albumin    Conformation    Microenvironment    Surface hydrophobicity  
本文献已被 CNKI 维普 万方数据 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号