Hydrophobic Volume Effects in Albumin Solutions.
Density measurements of aqueous albumin solutions as a function of concentration and temperature are reported. The solvents were H(2)O, D(2)O, and a physiological H(2)O-based buffer. An anomaly of the density at very small concentrations of albumin in D(2)O was found. Furthermore, the partial specific volume of albumin is remarkably different in D(2)O and H(2)O. We attribute both effects to structural differences of the solvents. Copyright 2001 Academic Press.
Schrade
P.
P
Institut för Raumsimulation, DLR, Cologne, 51170, Germany
Klein
H.
H
Egry
I.
Ademovic
Z.
Z
Klee
D.
D