The charge effects of the self-diffusion constant of bovine mercaptalbumin.
The charge effect on the translational self-diffusion constant, D, of polyelectrolytes has been quantitatively analyzed based on dynamic light scattering experiments. Perfectly monodisperse bovine mercaptalbumin has been used at low pH as a positively charged polyelectrolyte sample. Completely linear plots of log(g2(t)-1) vs. time t have been obtained for uncharged states of the protein, for the correlation function of the scattered light intensity, g2(t). The plots deviate from linearity as polyions bear the charges. The D values for various ionic states, obtained from the initial slopes of the plots, have been analyzed using the simple theory of Imai and Mandel (N. Imai and M. Mandel, Macromolecules 15 (1982) 1562) derived based on the Onsager-Navier-Stokes equation for solvent flow with counterion distribution around a polyion. It has turned out that the experimental D values coincide well with the theory and that the characteristic nature of D can be elucidated principally from the charge effect.
Hirakawa
F
F
Department of Physics, Faculty of Science, Nagoya University, Japan.
Yoshino
S
S
Era
S
S
Kuwata
K
K
Sogami
M
M
Imai
N
N
D004058:Diffusion; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008433:Mathematics; D012709:Serum Albumin; D012710:Serum Albumin, Bovine
D012709:Serum Albumin; C001702:mercaptoalbumin; D012710:Serum Albumin, Bovine