Optical probe study of a nonentangling macromolecule solution--bovine serum albumin: Water

Abstract

The diffusion coefficient D of polystyrene latex spheres in bovine serum albumin:water was studied as a function of protein concentration c for 0 c D fails by as much as 25 to 50%, D being larger than predicted from the sphere radius R and the solution viscosity. Probe particles with R as large as 0.62 [mu]m were used. D fits well to the form D = Doexp(-[alpha]cv) for [alpha] = 0.004 to 0.008 and v = 0.96 to 0.99. Serum albumin is a globular protein, so chain entanglement cannot cause these non-Stokes--Einsteinian effects, which are presumably due to sphere:albumin interactions. Polystyrene spheres in semidilute polyethylene oxide:water (G. S. Ullmann, K. Ullmann, R. M. Lindner, and G. D. J. Phillies, J. Phys. Chem. 89, 692 (1985)) behave similarly to spheres in serum albumin:water, suggesting that chain entanglement may also not be important in probe diffusion through semidilute polymer solutions.