Citation: Quan BAI, Yin Mao WEI, Ming Hui GENG, Xin Du GENG. High Performance Hydrophobic Interaction Chromatography-A New Approach to Separate Intermediates of Protein Folding Ⅰ. Separation of Intermediates of Urea-unfolded α-Amylase[J]. Chinese Chemical Letters, ;1997, 8(1): 67-70. shu

High Performance Hydrophobic Interaction Chromatography-A New Approach to Separate Intermediates of Protein Folding Ⅰ. Separation of Intermediates of Urea-unfolded α-Amylase

Institute of Modern Separation Science, Northwest University, Xi'an 710069

Received Date: 21 October 1996

Fund Project: The Project was supported by The National Science Foundation of China.

Based on the different hydrophobicities of the intermediates of proteins,the various conformational intermediates of the refolding of α-amylase originally denatured with 8.0 mol/L urea solution were separated with high performance hydrophobic interaction chromatography (HPHIC).Compared to the separation of the same intermediates with weak anion exchange chromatography and size-exclusion chromatography,the result obtained with HPHIC is the best.It would be expected that HPHIC may be a strongly potential tool to separate intermediates of some proteins which cannot be,or cannot completely be refolded by HPHIC.
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