Small-Angle X-Ray Studies of a Human Immunoglobulin M

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Abstract
The conformation of a Waldenstroem immunoglobulin(Ig)M with antibody-like activity for X-ray contrast media, based on 3-amino-2,4,6-triiodobenzoic acid, was studied by small-angle X-ray scattering. The radius of gyration was determined as 12.1 nm, the maximum distance was 35 nm and the volume was 1900 nm3. A flat star-shaped model was equivalent in scattering. Aggregation of IgM molecules seems to take place as side-by-side combinations of single molecules, manifesting itself as a relatively large increase of the radius of gyration and unchanged thickness of the flat aggregates.