A SUBCLASS OF HUMAN γA-GLOBULINS (γA2) WHICH LACKS THE DISULFIDE BONDS LINKING HEAVY AND LIGHT CHAINS

The γA2-subgroup of γA-globulins, previously delineated by antigenic studies, was found to differ strikingly from other immunoglobulins in the manner in which the polypeptide chains are bound together. The heavy and light chains were not linked to each other by disulfide bonds. Instead the light cha...

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Detalles Bibliográficos
Autores principales: Grey, Howard M., Abel, Carlos A., Yount, William J., Kunkel, Henry G.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1968
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138581/
https://www.ncbi.nlm.nih.gov/pubmed/4176936
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author Grey, Howard M.
Abel, Carlos A.
Yount, William J.
Kunkel, Henry G.
author_facet Grey, Howard M.
Abel, Carlos A.
Yount, William J.
Kunkel, Henry G.
author_sort Grey, Howard M.
collection PubMed
description The γA2-subgroup of γA-globulins, previously delineated by antigenic studies, was found to differ strikingly from other immunoglobulins in the manner in which the polypeptide chains are bound together. The heavy and light chains were not linked to each other by disulfide bonds. Instead the light chains were disulfide linked to one another, and were present in the γA2-molecule as disulfide bridged L-L dimers. Antisera specific for γA2-proteins indicated the occurrence of two different antigenic types in all normal sera as well as saliva and colostrum. Both of these showed the unique interchain disulfide linkage. Quantitative analyses indicated higher levels of γA2-proteins in external secretions.
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spelling pubmed-21385812008-04-17 A SUBCLASS OF HUMAN γA-GLOBULINS (γA2) WHICH LACKS THE DISULFIDE BONDS LINKING HEAVY AND LIGHT CHAINS Grey, Howard M. Abel, Carlos A. Yount, William J. Kunkel, Henry G. J Exp Med Article The γA2-subgroup of γA-globulins, previously delineated by antigenic studies, was found to differ strikingly from other immunoglobulins in the manner in which the polypeptide chains are bound together. The heavy and light chains were not linked to each other by disulfide bonds. Instead the light chains were disulfide linked to one another, and were present in the γA2-molecule as disulfide bridged L-L dimers. Antisera specific for γA2-proteins indicated the occurrence of two different antigenic types in all normal sera as well as saliva and colostrum. Both of these showed the unique interchain disulfide linkage. Quantitative analyses indicated higher levels of γA2-proteins in external secretions. The Rockefeller University Press 1968-11-30 /pmc/articles/PMC2138581/ /pubmed/4176936 Text en Copyright © 1968 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
Grey, Howard M.
Abel, Carlos A.
Yount, William J.
Kunkel, Henry G.
A SUBCLASS OF HUMAN γA-GLOBULINS (γA2) WHICH LACKS THE DISULFIDE BONDS LINKING HEAVY AND LIGHT CHAINS
title A SUBCLASS OF HUMAN γA-GLOBULINS (γA2) WHICH LACKS THE DISULFIDE BONDS LINKING HEAVY AND LIGHT CHAINS
title_full A SUBCLASS OF HUMAN γA-GLOBULINS (γA2) WHICH LACKS THE DISULFIDE BONDS LINKING HEAVY AND LIGHT CHAINS
title_fullStr A SUBCLASS OF HUMAN γA-GLOBULINS (γA2) WHICH LACKS THE DISULFIDE BONDS LINKING HEAVY AND LIGHT CHAINS
title_full_unstemmed A SUBCLASS OF HUMAN γA-GLOBULINS (γA2) WHICH LACKS THE DISULFIDE BONDS LINKING HEAVY AND LIGHT CHAINS
title_short A SUBCLASS OF HUMAN γA-GLOBULINS (γA2) WHICH LACKS THE DISULFIDE BONDS LINKING HEAVY AND LIGHT CHAINS
title_sort subclass of human γa-globulins (γa2) which lacks the disulfide bonds linking heavy and light chains
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138581/
https://www.ncbi.nlm.nih.gov/pubmed/4176936
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