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QUANTITATIVE VARIATIONS IN L CHAIN TYPES IN GUINEA PIG ANTIHAPTEN ANTIBODIES
In guinea pig purified antihapten antibodies, the proportion of molecules bearing the κ- or λ-type of L chains (K or L molecules) may diverge markedly from that found in normal γ(2)-globulins. This has been evaluated by precipitation of I(131)-labeled antibody preparations using a specific anti-λ-ch...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1966
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138265/ https://www.ncbi.nlm.nih.gov/pubmed/4162733 |
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author | Nussenzweig, Victor Benacerraf, Baruj |
author_facet | Nussenzweig, Victor Benacerraf, Baruj |
author_sort | Nussenzweig, Victor |
collection | PubMed |
description | In guinea pig purified antihapten antibodies, the proportion of molecules bearing the κ- or λ-type of L chains (K or L molecules) may diverge markedly from that found in normal γ(2)-globulins. This has been evaluated by precipitation of I(131)-labeled antibody preparations using a specific anti-λ-chain antiserum. Anti-DNP antibodies isolated 3 wk after immunization of guinea pigs with DNP(65)-BGG antibodies, contain less than 1% of L molecules, while in pipsyl antibodies, isolated from the sera of animals immunized with pipsyl-BGG, the proportion of L molecules is significantly greater than in normal γ(2)-globulins. Anti-DNP antibodies produced against conjugates of this hapten with carriers other than BGG (BSA, OVA, or poly-L-lysine) or with BGG with a small number of DNP groups (DNP(10)-BGG) contained a greater proportion of λ-chain bearing molecules than anti-DNP antibodies isolated from late sera of guinea pigs immunized with highly conjugated DNP(65)-BGG. An increased percentage of L molecules was detected in preparations of anti-DNP(65)-BGG antibodies isolated early (10 days), when compared to those isolated later during the course of immunization. However, the level of L molecules in all these anti-DNP antibody preparations was always considerably below that present in normal γ(2)-globulin. The relative amounts of L molecules in distinct immunoglobulin families (γ(1) and γ(2)) in antibody preparations isolated from individual animals was remarkably similar. |
format | Text |
id | pubmed-2138265 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1966 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21382652008-04-17 QUANTITATIVE VARIATIONS IN L CHAIN TYPES IN GUINEA PIG ANTIHAPTEN ANTIBODIES Nussenzweig, Victor Benacerraf, Baruj J Exp Med Article In guinea pig purified antihapten antibodies, the proportion of molecules bearing the κ- or λ-type of L chains (K or L molecules) may diverge markedly from that found in normal γ(2)-globulins. This has been evaluated by precipitation of I(131)-labeled antibody preparations using a specific anti-λ-chain antiserum. Anti-DNP antibodies isolated 3 wk after immunization of guinea pigs with DNP(65)-BGG antibodies, contain less than 1% of L molecules, while in pipsyl antibodies, isolated from the sera of animals immunized with pipsyl-BGG, the proportion of L molecules is significantly greater than in normal γ(2)-globulins. Anti-DNP antibodies produced against conjugates of this hapten with carriers other than BGG (BSA, OVA, or poly-L-lysine) or with BGG with a small number of DNP groups (DNP(10)-BGG) contained a greater proportion of λ-chain bearing molecules than anti-DNP antibodies isolated from late sera of guinea pigs immunized with highly conjugated DNP(65)-BGG. An increased percentage of L molecules was detected in preparations of anti-DNP(65)-BGG antibodies isolated early (10 days), when compared to those isolated later during the course of immunization. However, the level of L molecules in all these anti-DNP antibody preparations was always considerably below that present in normal γ(2)-globulin. The relative amounts of L molecules in distinct immunoglobulin families (γ(1) and γ(2)) in antibody preparations isolated from individual animals was remarkably similar. The Rockefeller University Press 1966-10-31 /pmc/articles/PMC2138265/ /pubmed/4162733 Text en Copyright © 1966 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 Nussenzweig, Victor Benacerraf, Baruj QUANTITATIVE VARIATIONS IN L CHAIN TYPES IN GUINEA PIG ANTIHAPTEN ANTIBODIES |
title | QUANTITATIVE VARIATIONS IN L CHAIN TYPES IN GUINEA PIG ANTIHAPTEN ANTIBODIES |
title_full | QUANTITATIVE VARIATIONS IN L CHAIN TYPES IN GUINEA PIG ANTIHAPTEN ANTIBODIES |
title_fullStr | QUANTITATIVE VARIATIONS IN L CHAIN TYPES IN GUINEA PIG ANTIHAPTEN ANTIBODIES |
title_full_unstemmed | QUANTITATIVE VARIATIONS IN L CHAIN TYPES IN GUINEA PIG ANTIHAPTEN ANTIBODIES |
title_short | QUANTITATIVE VARIATIONS IN L CHAIN TYPES IN GUINEA PIG ANTIHAPTEN ANTIBODIES |
title_sort | quantitative variations in l chain types in guinea pig antihapten antibodies |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2138265/ https://www.ncbi.nlm.nih.gov/pubmed/4162733 |
work_keys_str_mv | AT nussenzweigvictor quantitativevariationsinlchaintypesinguineapigantihaptenantibodies AT benacerrafbaruj quantitativevariationsinlchaintypesinguineapigantihaptenantibodies |