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Presence of interchain disulfide bonds between two gene products that compose the secreted form of an antigen-specific suppressor factor
The secreted form of the suppressor T cell factor specific for keyhole limpet hemocyanin derived from the hybridoma 34S-704 was found to consist of the two distinct polypeptide chains, i.e., the antigen- binding and the I-J-encoded chains. They were linked in covalent association with disulfide bond...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1981
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2186189/ https://www.ncbi.nlm.nih.gov/pubmed/6166720 |
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collection | PubMed |
description | The secreted form of the suppressor T cell factor specific for keyhole limpet hemocyanin derived from the hybridoma 34S-704 was found to consist of the two distinct polypeptide chains, i.e., the antigen- binding and the I-J-encoded chains. They were linked in covalent association with disulfide bonds. The two chains were cleaved by the reduction with dithiothreitol and were easy to reconstitute the active form of TsF. The association of the two distinct chains was suggested to be essential for the expression of the TsF activity. |
format | Text |
id | pubmed-2186189 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1981 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21861892008-04-17 Presence of interchain disulfide bonds between two gene products that compose the secreted form of an antigen-specific suppressor factor J Exp Med Articles The secreted form of the suppressor T cell factor specific for keyhole limpet hemocyanin derived from the hybridoma 34S-704 was found to consist of the two distinct polypeptide chains, i.e., the antigen- binding and the I-J-encoded chains. They were linked in covalent association with disulfide bonds. The two chains were cleaved by the reduction with dithiothreitol and were easy to reconstitute the active form of TsF. The association of the two distinct chains was suggested to be essential for the expression of the TsF activity. The Rockefeller University Press 1981-06-01 /pmc/articles/PMC2186189/ /pubmed/6166720 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 Presence of interchain disulfide bonds between two gene products that compose the secreted form of an antigen-specific suppressor factor |
title | Presence of interchain disulfide bonds between two gene products that compose the secreted form of an antigen-specific suppressor factor |
title_full | Presence of interchain disulfide bonds between two gene products that compose the secreted form of an antigen-specific suppressor factor |
title_fullStr | Presence of interchain disulfide bonds between two gene products that compose the secreted form of an antigen-specific suppressor factor |
title_full_unstemmed | Presence of interchain disulfide bonds between two gene products that compose the secreted form of an antigen-specific suppressor factor |
title_short | Presence of interchain disulfide bonds between two gene products that compose the secreted form of an antigen-specific suppressor factor |
title_sort | presence of interchain disulfide bonds between two gene products that compose the secreted form of an antigen-specific suppressor factor |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2186189/ https://www.ncbi.nlm.nih.gov/pubmed/6166720 |