Abstract
A large amount of evidence has been reported to support the view that anions combine with positive groups on the albumin molecule. Therefore, anion-protein interaction in the range of pH 5.2 to 12.0 would involve the imidazolium groups of the histidine residues, the guanidinium groups of the arginine residues and the ∈-ammonium groups of the lysine residues of bovine plasma albumin molecule. In this paper, there is made the comparative study of the interactions of some food azo-dyes (Ponceau R, New Coccine and Orange G) and isoxanthene dyes (Erythrosine, Eosine, Phloxine and Rose Bengale) with native bovine plasma albumin. The study of these interactions after the modification of the protein molecule by the removal of these positive charges by different pH's may give information concerning the identification of the binding sites and in this paper the results, too, are reported.
