タンパク質の沈殿剤について

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Protein solubility is a function of such a factor as pH, ionic strength, temperature, presence or absence of additive (e.g. salt) and kind and concentration of the additive. Inorganic salts are known to affect the protein solubility in widely different manner. Certain salts, e.g. Na2SO4 and (NH4)2SO4, and organic solvents such as acetone, alcohol and polyethylene glycol are frequently used to precipitate or crystallize proteins. To eluci- date the effect of such additives on the protein solubility, study on preferential interactions of proteins with solvent components in water/protein/additive system has been carried out. In this review, concept of the preferential interaction and thermodynamic analysis of the protein solubility on the basis of the preferential interaction are introduced. In addition, typical data of the preferential interaction measurements were summerized, showing a correlation between the protein solvent interaction and the effect of solvent additive on the protein solubility. The salting-out effects of certain salts, polyethylene glycol and hexylene glycol were interpreted in terms of the unfavorable interaction between proteins and theseadditives, favoring a state in which the interaction is reduced and therefore more contacts between protein molecules are formed. From the protein solvent interactions and the measurements of protein stability, it was pointed out that these additives are different in their effects on the protein stability.
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タンパク質の沈殿剤について

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