Abstract
Unreduced egg albumin was titrated at 0.025 and 0.20 ionic strength with sodium dodecylsulfate using a microcalorimeter to follow the reaction. Evidence was obtained for two classes of Na dodecylsulfate binding sites at the lower ionic strength, one saturating at 0.4 g of detergent per gram of protein, the other saturating at 1.4 g/g. Some additional Na dodecylsulfate was apparently bound at the higher ionic strength. The apparent average enthalpy per mole of Na dodecylsulfate bound was about 30% lower for the 0–0.4 g/g and 0.4–1.4 g/g classes of Na dodecylsulfate binding sites at 0.20 ionic strength. The Na dodecylsulfate binding appeared to be highly cooperative. The average overall enthalpies found were 1.1 kcal/mole of Na dodecylsulfate bound or less, indicating that the binding of Na dodecylsulfate to egg albumin is an entropy-driven reaction.
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