Abstract
Heat effects and densities of bovine albumin solutions in Na-acetate buffer pH 4.2 at various NaCl, Li2SO4 and (NH4)2SO4 concentrations were determined by a LKB 10700-2 microcalorimeter and an Anton Paar 60/602 densimeter (25°C). The density measurements were made after 1 and 48 h of the dissolution of bovine albumin in the buffer. The correlations between the changes of the enthalpy of salting and apparent molar volumes vs. concentrations of salts were determined.
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