Spectroscopic Studies on the Mechanism of Interaction between Vitamin B12 and Vitamin C with Bovine Serum Albumin
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The interaction between vitamin C and vitamin B12 with bovine serum albumin has been investigated. The binding mechanism was studied by UV-absorption and fluorescence spectroscopy. From spectral analysis both vitamins showed strong ability to quench the intrinsic fluorescence of BSA through a static quenching procedure. The binding constants are estimated to be 1.39 x 104 M-1 for vitamin C and 1.61 x 104 M-1 for vitamin B12. FT-IR spectroscopy was used to determine the protein secondary structure. The observed spectral changes indicates an increase of intensity for HSA-vitamin C interaction and a reduction of intensity for HSA-vitamin B12 interaction. While in the difference spectra of vitamin B12-BSA complexes, intensity decreases as the concentration of vitamin B12 increases for amide I. This variation of intensity is related indirectly to the formation of H-bonding in the complex molecules.