Abstract
8S monomeric subunit of a human immunoglobulin M was investigated by small-angle X-ray scattering. The following molecular parameters were determined: radius of gyration 5.9 nm, maximum length 21 nm, hydrated volume 410 nm 3 and two radii of gyration of the cross-section: 2.6 and 1.8 nm. A model equivalent in scattering was found and compared with the model for a human IgG also based on small-angle X-ray scattering data. The Cμ2 domain of the IgM obviously has a very loose structure, and the Fab angle of the 8S IgM (90°) is smaller than that of the IgG (134°).
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