FURTHER STUDIES ON THE ULTRASTRUCTURE OF DIMERIC IGA OF HUMAN ORIGIN

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....

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Detalles Bibliográficos
Autores principales: Bloth, Björn, Svehag, Sven-Eric
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1971
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138909/
https://www.ncbi.nlm.nih.gov/pubmed/4995063
Descripción
Sumario: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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