Spectrophotometric Studies On The Interaction Of Bovine Serum Albumin With Triphenylmethane Dyes
Spectrophotometric studies on the interaction of three triphenylmethane dyes, bromophenol blue, coomassie brilliant blue R250 and thymol blue with bovine serum albumin have been reported. Data has been analyzed for spectral shifts, extent of combination, composition of complexes, association constants and number of binding sites. Spectral shifts indicated that dyes interact with cationic groups on the protein molecule. Association constants varied between 2.7x104 to 2.3x105, consistent with non-covalent interactions. The number of binding sites varied between 2 and 3 for different dyes. All basic amino acid resdues in protein were not accessible to the dye at pH 2.5.