Studies on the Various Refolded Intermediates of α-Amylase Denatured by Urea with High Performance Hydrophobic Interaction Chromatography

Abstract

Abstract: a-Amylase originally denatured with 8.0mol/Lurea 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.

Key words: Hydrophobic interaction chromatography, Protein folding, Refolded intermediate, Separation, α-Amylase

CLC Number:

O657.7

TrendMD:

BAI Quan, WEI Yin-Mao, GENG Ming-Hui, GENG Xin-Du . Studies on the Various Refolded Intermediates of α-Amylase Denatured by Urea with High Performance Hydrophobic Interaction Chromatography[J]. Chem. J. Chinese Universities, 1997, 18(8): 1291.

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Studies on the Various Refolded Intermediates of α-Amylase Denatured by Urea with High Performance Hydrophobic Interaction Chromatography

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