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作 者:Xindu Geng Jing Zhang Yinmao Wei
出 处:《Chinese Science Bulletin》2000年第3期237-241,共5页
摘 要:Based on the fact that the stoichiometric displacement model for retention of solute and the total adsorption free energy of solute on a solid surface can be divided into two components, net adsorption and net desorbed energies, a new principle and an equation for calculating the free energy of protein folding, △△GF, on the solid surface are proposed. With high-performance hydrophobic interaction chromatography (HPHIC), an experimental method for determining the △△GF is established. Lysozyme and a-amylase have been selected as examples to test the new method, and their △△GF on the HPHIC stationary phase surface are found to be much higher than that reported from a solution. In addition, the △△GF of the two proteins are found to increase with the concentration of denaturing agent employed. The average standard deviations,±4.7% for lysozyme and ± 3.0% for a-amylase, indicate that the new method has a satisfactory reproducibility and reliability.Based on the fact that the stoichiometric displacement model for retention of solute and the total adsorption free energy of solute on a solid surface can be divided into two components, net adsorption and net desorbed energies, a new principle and an equation for calculating the free energy of protein folding, ΔΔGF, on the solid surface are proposed. With high-performance hydrophobic interaction chromatography (HPHIC), an experimental method for determining the ΔΔGF is established. Lysozyme and α-amylase have been selected as examples to test the new method, and their ΔΔGF on the HPHIC stationary phase surface are found to be much higher than that reported from a solution. In addition, the ΔΔGF of the two proteins are found to increase with the concentration of denaturing agent employed. The average standard deviations, ±4.7% for lysozyme and ±3.0% for α-amylase, indicate that the new method has a satisfactory reproducibility and reliability.
关 键 词:STOICHIOMETRIC displacement model high-performance HYDROPHOBIC interaction CHROMATOGRAPHY adsorption free energy protein folding.
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