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Combinatorial Analysis of the Conformational Transition of Bacillus Amyloliquefaciensα-Amylase during Urea-induced Unfolding and Refolding

YANG Wen-hui;JI Xu;BIAN Liu-jiao;College of Life Science,Northwest University;  
The urea-induced unfolding and refolding of Bacillus amyloliquefaciensα-amylases was investigated through the combination of protein electrophoresis,size exclusion chromatography,intrinsic fluorescence emission spectroscopy,fluorescence phase diagram,fluorescence quenching and biological activity assay.The results showed that during the unfolding and refolding ofα-amylase induced by urea,theα-amylase molecules existed only in the unimolecular form instead of aggregate or aggregate precipitation,apartially folded intermediate separately occurred at about 4.0mol/L urea in the unfolding and refolding processes and both of the unfolding and refolding followed a three-state model.Additionally,the deactivation curve was nearly identical to the renaturation curve in urea solutions.Combining with previous studies about the unfolding and refolding of Bacillus amyloliquefaciensα-amylases induced by guanidine hydrochloride,it can be inferred that the unfolding and refolding ofα-amylase induced by urea and guanidine hydrochloride are separately a mutually reversible procedure.
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