6533b82efe1ef96bd1293aaa

RESEARCH PRODUCT

Preferential solvation of lysozyme and bovine serum albumin in copper salt solutions. A quantitative chromatographic study

A. ZatonC. AbadM. Trueba

subject

ChromatographybiologyInorganic chemistrySerum albuminSolvationInorganic ChemistryGel permeation chromatographyMetalchemistry.chemical_compoundAdsorptionchemistryvisual_artMaterials Chemistrybiology.proteinvisual_art.visual_art_mediumPhysical and Theoretical ChemistryLysozymeBovine serum albuminRefractometry

description

Preferential solvation λ parameters for systems containing water-copper salt-protein (lysozyme or bovine serum albumin) have been determined by gel permeation chromatography. When water is preferentially adsorbed by the protein, good agreement is found between λ values determined by this method and by equilibrium dialysis-differential refractometry. The influence of the concentration and type of anion component of the copper salt, protein concentration and temperature has been investigated. The methodology used also allows direct visualization of the metal ion bound to the protein and to determine binding parameters. Apparent association constants of 2.0 × 102 M−1 and 1.7 × 102 M−1 have been obtained for the binding of copper nitrate to lysozyme at 30 and 4 °C, respectively.

https://doi.org/10.1016/s0020-1693(00)83295-8