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Lymphocyte activation by monovalent fragments of antibodies reactive with cell surface carbohydrates
Antibodies reactive with cell surface carbohydrates were isolated from normal chicken serum and were found to be mitogenic for mouse splenic lymphocytes as assayed by both blast transformation and [3H]thymidine incorporation. The Fab' fragments of these carbohydrate-binding immunoglobulins were...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1976
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2190129/ https://www.ncbi.nlm.nih.gov/pubmed/1249523 |
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collection | PubMed |
description | Antibodies reactive with cell surface carbohydrates were isolated from normal chicken serum and were found to be mitogenic for mouse splenic lymphocytes as assayed by both blast transformation and [3H]thymidine incorporation. The Fab' fragments of these carbohydrate-binding immunoglobulins were just as mitogenic as the divalent native antibody. Moreover, succinylated Fab' fragments, which probably would not form self-associating aggregates, showed similar mitogenic properties. All of these results indicate that, at least for saccharide-specific ligands, multipoint attachment and receptor cross-linkage on the cell to which the ligand is attached may not be a stringent requirement for activation. |
format | Text |
id | pubmed-2190129 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1976 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21901292008-04-17 Lymphocyte activation by monovalent fragments of antibodies reactive with cell surface carbohydrates J Exp Med Articles Antibodies reactive with cell surface carbohydrates were isolated from normal chicken serum and were found to be mitogenic for mouse splenic lymphocytes as assayed by both blast transformation and [3H]thymidine incorporation. The Fab' fragments of these carbohydrate-binding immunoglobulins were just as mitogenic as the divalent native antibody. Moreover, succinylated Fab' fragments, which probably would not form self-associating aggregates, showed similar mitogenic properties. All of these results indicate that, at least for saccharide-specific ligands, multipoint attachment and receptor cross-linkage on the cell to which the ligand is attached may not be a stringent requirement for activation. The Rockefeller University Press 1976-03-01 /pmc/articles/PMC2190129/ /pubmed/1249523 Text en 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 | Articles Lymphocyte activation by monovalent fragments of antibodies reactive with cell surface carbohydrates |
title | Lymphocyte activation by monovalent fragments of antibodies reactive with cell surface carbohydrates |
title_full | Lymphocyte activation by monovalent fragments of antibodies reactive with cell surface carbohydrates |
title_fullStr | Lymphocyte activation by monovalent fragments of antibodies reactive with cell surface carbohydrates |
title_full_unstemmed | Lymphocyte activation by monovalent fragments of antibodies reactive with cell surface carbohydrates |
title_short | Lymphocyte activation by monovalent fragments of antibodies reactive with cell surface carbohydrates |
title_sort | lymphocyte activation by monovalent fragments of antibodies reactive with cell surface carbohydrates |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2190129/ https://www.ncbi.nlm.nih.gov/pubmed/1249523 |