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Determination of the adsorption isotherms of denatured lysozyme by changes of the concentration of guanidine hydrochloride(50-01-1)

The adsorption isotherm of the modified lysozyme(Lys) at different temperatures on the surface of the hydrophobic chromatographic filler PEG 600 was determined by changing the guanidine hydrochloride(50-01-1) concentration and the concentration of lysozyme. The results showed that the adsorption was at 25 ℃, 35 ℃ and 45 ℃. The time required for equilibration is 5h, 4h and 2h, respectively. The reason may be that the coating effect is obvious at 25 ℃. When the temperature is increased, the coating effect disappears and the adsorption is easy to reach equilibrium. When the concentration of guanidine hydrochloride(50-01-1) is changed, (Ie, at least a perturbation), suggesting that the protein may undergo a conformation mutation (at least perturbation). The adsorption of metamorphism is at least 0.8%. The linear relationship between the SDM A and the adsorption isotherm of lysozyme is very good, indicating that SDM A is suitable for the adsorption of lysozyme on the liquid - solid interface.



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