The kinetics of soluble aggregate formation in equine IgG was studied
in the pH 3.4-4.3 range and ionic strength between 0.02 and 0.5 M, and
a diagram describing aggregation kinetics as diffusion limited, react
ion limited, or transitional as a function of pH and ionic strength wa
s constructed. Aggregation rate is limited by the degree of electrosta
tic repulsion between the protein molecules in the pH 4.0-4.5 range. B
elow pH 4.0, a greater degree of attractive force is present, most lik
ely from protein unfolding, and electrostatic repulsion no longer dete
rmines the rate of aggregation. The aggregation rate increases with de
creasing pH, and at pH 3.4 the aggregation rate is diffusion limited.
The pH range separating reaction-limited and diffusion-limited kinetic
s decreases with increasing ionic strength, indicating charge shieldin
g from the buffer solution influences the aggregation rate. (C) 1997 A
cademic Press.