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. 1971 May 1;133(5):1035-42.
doi: 10.1084/jem.133.5.1035.

Further studies on the ultrastructure of dimeric IgA of human origin

B Bloth, S E Svehag

Further studies on the ultrastructure of dimeric IgA of human origin

B Bloth et al. J Exp Med. .

Abstract

Human colostral IgA and myeloma dimer IgA were purified and examined in the electron microscope using a modified technique of negative staining. Both types of preparation contained double Y-shaped structures of the dimensions: Fab region, 35 x 70 A, and the sum of the two Fc regions, 40 x 140-155 A. Colostral IgA as well as myeloma dimer IgA molecules showed a tendency of bending at the point where the Fc regions joined. Secretory component bound to dimer IgA produced no visible alteration of the molecule. Mild reduction and alkylation of colostral IgA yielded single Y-shaped 7S monomers with the dimensions, Fab, 35 x 70 A, and Fc, 40 x 65-70 A.

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