Abstract
The interaction of glycinin with urea/guanidine hydrochloride was investigated by determining the apparent partial specific volume of the protein in these solvents. The apparent partial specific volume was determined under both isomolal and isopotential conditions. The preferential interaction parameter with solvent components had values of 0.10 and 0.11 g urea and guanidine hydrochloride respectively per g of protein. In both the cases the interaction was not preferential with water. The total binding of urea/guanidine hydrochloride to glycinin was calculated. Excellent correlation between the calculated value and the total number of peptide bonds and aromatic amino acids residues of protein was observed. The changes in volume upon transferring glycinin from dilute salt solution to urea and guanidine hydrochloride solution were also calculated.
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