Preferential interaction and hydration parameters of human serum album
in (HSA) as a function of urea concentration in the entire solubility
range are obtained by partial specific volume measurements, At lower c
oncentrations (< 2 M) of urea, HSA exists in a molten globule state wi
th an unusually hydrated structure and increased Stokes radius, Differ
ential mechanism of interaction of urea at low and high concentrations
with HSA exists, This is in tune and conformity with the first observ
ation made by Prakash and Timasheff for other proteins.