Studies of Bovine Serum Albumin In Aqueous Solutions of some Salts Investigated By Ultrasonic Velocity, Viscosity and Density Measurements at 303.15K.

Interaction of Bovine Serum Albumin with Aqueous Solutions of Salts

Abstract

Ultrasonic velocity (u), densities (ρ)and viscosities (η) of (BSA) have been measured in the protein concentrationrange between 0.00125 to 0.04 g cm-3 at  303.15 K in water and water containing fixedconcentration 0.1480 mol dm-3 of salts like potassium oxalate ,sodium benzoate, cupric acetate, ammonium thiocyanate. The variation of u, ρ, ηand isentropic compressibility (Ks) as a function of proteinconcentration (C) in all cases is non linear. The relaxation time in all thesecases increases with increase of BSA concentration which indicates that thereis strong interaction of protein with these salts .The values of u, ρ and ηincrease with increasing concentration  of BSA.