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The small-angle x-ray scattering of solutions of rabbits IgG antibodies and their derivatives has been investigated. The reduction and alkylation of the native antibody cause a small increase of the molecular parameters, indicating a limited expansion of the molecule. Binding of native antipoly(D-alanyl) antibodies with hapten (80% saturation) causes a significant change of the quaternary structure, expressed by a decrease in the maximum diameter of about 2 nm, of the radius of gyration by 5.5%, and of the volume. The same antibodies, in which the single inter-heavy-chain disulfide bridge was opened by reduction and carboxamidomethylation, do not show any significant decrease in the overall molecular parameters upon reaction with hapten, except for a local structural change in a part of the molecule. These data lend further support to the notion that binding of hapten induces a conformational transition in its specific antibodies and suggest that the opening of the interchain disulfide bridges affects that transition. The dimensions of the intact antibodies calculated from measurements of small-angle x-ray scattering at low concentrations agree closely with those obtained from crystallographic studies.

proceedings of the national academy of sciences of the united states of america

Effect of cleaving interchain disulfide bridges on the radius of gyration and maximum length of anti-poly(D-alanyl) antibodies before and after reaction with tetraalanine hapten.