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
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author Bloth, Björn
Svehag, Sven-Eric
author_facet Bloth, Björn
Svehag, Sven-Eric
author_sort Bloth, Björn
collection PubMed
description 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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spelling pubmed-21389092008-04-17 FURTHER STUDIES ON THE ULTRASTRUCTURE OF DIMERIC IGA OF HUMAN ORIGIN Bloth, Björn Svehag, Sven-Eric J Exp Med Article 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. The Rockefeller University Press 1971-05-01 /pmc/articles/PMC2138909/ /pubmed/4995063 Text en Copyright © 1971 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Bloth, Björn
Svehag, Sven-Eric
FURTHER STUDIES ON THE ULTRASTRUCTURE OF DIMERIC IGA OF HUMAN ORIGIN
title FURTHER STUDIES ON THE ULTRASTRUCTURE OF DIMERIC IGA OF HUMAN ORIGIN
title_full FURTHER STUDIES ON THE ULTRASTRUCTURE OF DIMERIC IGA OF HUMAN ORIGIN
title_fullStr FURTHER STUDIES ON THE ULTRASTRUCTURE OF DIMERIC IGA OF HUMAN ORIGIN
title_full_unstemmed FURTHER STUDIES ON THE ULTRASTRUCTURE OF DIMERIC IGA OF HUMAN ORIGIN
title_short FURTHER STUDIES ON THE ULTRASTRUCTURE OF DIMERIC IGA OF HUMAN ORIGIN
title_sort further studies on the ultrastructure of dimeric iga of human origin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138909/
https://www.ncbi.nlm.nih.gov/pubmed/4995063
work_keys_str_mv AT blothbjorn furtherstudiesontheultrastructureofdimericigaofhumanorigin
AT svehagsveneric furtherstudiesontheultrastructureofdimericigaofhumanorigin

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