Abstract
Ultracentrifugation and fluorescence depolarization studies of chicken 7S IgG were designed to determine if high salt or high proton concentration induced polar orientation of the antibody active sites, facilitating lattice formation with antigen. Conditions of high proton concentration (pH 5·0) were used since at this pH, fowl antibody does not aggregate and the 7S form precipitates with homologous antigen. Ultracentrifugation studies with chicken anti-DNP IgG based on changing the pH of the solvent from 8·0 to 5·0, showed a significant decrease in the S 20.w value and an increase in the frictional ratio of 11 per cent. Fluorescnece depolarization data gave rotational data gave rotational relaxation times (ϱ) of 354 and 238 nsec for chicke IgG at pH 8·0 and 5·0 respectively. Both the increased frictional ratio and decreased rotational relaxation times, relative to the change in environment of the chicken IgG molecule from pH 8·0 to 5·0 are indicative of unfolding.
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