Shape of Immunoglobulins

HTT trypsin + urea Papain Papain Pepsin Pepsin Papain+ chymotrypsin C+ trypsin 

1970 Pilz et al., 1970 Valentine and Green, 1967). It appears to vary between 0 and 180°, the larger angles existing in the unliganded molecule. 

Optical rotatory dispersion (ORD) of immunoglobulins demonstrated a lack of a helix in earlier studies (Imahori and Momoi, 1962 Jirgensons, 1961 Winkler and Doty, 1961) and suggested the presence of some degree 

Information concerning the binding site of antibodies has recently been obtained from the X-ray studies (Amzel et aL, 1974 Segal et aL, 1974). Both the human myeloma NEW and the mouse myeloma IgA McPC603 are known to bind haptens. In both cases the antigen-binding site is at the end of the Fab fragment exposed to solvent and formed by 

The spiderlike arrangement (Chesebro et al., 1968) of IgM has already been mentioned. The CD spectrum of the isolated Fab fragment is similar to that of the IgG Fab, but the Fc fragments of the two classes differ (Ghose, 1971), the Fc CD spectra showing greater amounts of )8 structure than Fcy. 

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Figure 8.11a. The shape of immunoglobulin G. Adapted from C. Branden and J. Toozet ].

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