Importance of the nature of anions in lysozyme crystallisation correlated with protein net charge variation.
Hofmeister anion series are studied to examine the coupled influence of pH and ionic strength on the solubility of previously desalted lysozyme. Solubility curves are measured at pH 4.3 and 8.3 and 18 degrees C for nitrate, para-toluenesulfonate, citrate, sulphate, phosphate, and acetate. Extreme low ionic strength is explored, confirming the decrease of lysozyme solubility while increasing the protein net charge and the ionic strength. The classification of specific salt effects takes into account the valence of the anions with respect to the protein net charge.
D000818:Animals; D000838:Anions; D003460:Crystallization; D004563:Electrochemistry; D006863:Hydrogen-Ion Concentration; D009113:Muramidase / Q000737:chemistry*; D009994:Osmolar Concentration; D012995:Solubility
D000838:Anions; D009113:Muramidase