Abstract
The interaction between molybdate ions and bovine serum albumin (BSA) has been studied employing transmittance measurements. In the acidic range, the stoichiometry of the combination between molybdate and protonated nitrogen groups of protein was found to be one-to-one. The pH-dependent binding result has been ascribed to the existence of anionic as well as cationic species of molybdenum(VI). The pH-metric titrations and ultraviolet absorption spectra of molybdenum(VI)-bovine serum albumin mixtures also supported the existence of polymerisation-depolymerisation of molybdenum as well as deprotonation and conformational changes in the protein molecule. The free energy, enthalpy and entropy of binding have been determined and the effect of molybdate ion on the heat of ionization and p K int. of BSA groups has' been discussed.
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