摘要
用高效疏水色谱法对用脲变性的α-淀粉酶的体外折叠中间体进行了分离，发现脲变α-淀粉酶折叠至少有19个中间体，而且，这些中间体在色谱流出液中可稳定一周．这一结论已由电泳、离子交换色谱和体积排阻色谱法证实．此外，还用紫外吸收光谱和荧光发射光谱研究了这些折叠中间体与天然α-淀粉酶构象之间的差异．
a-Amylase originally denatured with 8.0mol/L urea and its re folded intermedi-ates were investigated by high performance hydrophobic interaction chromatography. Many kinds(at least 19) of its re folded intermediates were obtained and found to be relatively sta-ble, at least for a week, in their respective solutions of the mobile phase used. The result was further proved by the methods of electrophoresis, ion exchange chromatography and size exclusive chromatography. In addition, the difference between the molecular conformations of these intermediates was investigated by ultraviolet-absorption spectrum and fluorescence emission spectrum.
出处
《高等学校化学学报》
SCIE
EI
CAS
CSCD
北大核心
1997年第8期1291-1295,共5页
Chemical Journal of Chinese Universities
基金
国家自然科学基金
关键词
蛋白折叠
折叠中间体
Α淀粉酶
HPHIC
α-Amy
Hydrophobic interaction chromatography, Protein folding, Refolded intermediate, Separation, α-Amylase
