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Structural and functional differences between the H-2 controlled Ss and Slp proteins
Based on functional and structural data, it is concluded that the Ss protein in the mouse expresses the activity of the fourth component of complement. Removal of the Ss, but not of Slp, antigen correlates with a high degree of significance (P less than 0.001) with decrease of C4 hemolytic activity....
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1978
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2185059/ https://www.ncbi.nlm.nih.gov/pubmed/722239 |
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collection | PubMed |
description | Based on functional and structural data, it is concluded that the Ss protein in the mouse expresses the activity of the fourth component of complement. Removal of the Ss, but not of Slp, antigen correlates with a high degree of significance (P less than 0.001) with decrease of C4 hemolytic activity. In phenotypically Slp negative mice the plasma/serum levels of Ss correlate with the C4 activity (P less than 0.001). Structurally, Ss is a 209,000-mol wt protein, consisting of three covalently linked polypeptide chains (alpha,beta,gamma). Treatment of Ss with C1 cleaves a 7,000-8,000-mol wt fragment from the alpha-chain. Slp is also a three chain covalently linked protein of 209,000 daltons, however its three chains differ in size from those of the Ss protein. Slp does not express hemolytic activity and its alpha- chain is not cleaved by C1. |
format | Text |
id | pubmed-2185059 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1978 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21850592008-04-17 Structural and functional differences between the H-2 controlled Ss and Slp proteins J Exp Med Articles Based on functional and structural data, it is concluded that the Ss protein in the mouse expresses the activity of the fourth component of complement. Removal of the Ss, but not of Slp, antigen correlates with a high degree of significance (P less than 0.001) with decrease of C4 hemolytic activity. In phenotypically Slp negative mice the plasma/serum levels of Ss correlate with the C4 activity (P less than 0.001). Structurally, Ss is a 209,000-mol wt protein, consisting of three covalently linked polypeptide chains (alpha,beta,gamma). Treatment of Ss with C1 cleaves a 7,000-8,000-mol wt fragment from the alpha-chain. Slp is also a three chain covalently linked protein of 209,000 daltons, however its three chains differ in size from those of the Ss protein. Slp does not express hemolytic activity and its alpha- chain is not cleaved by C1. The Rockefeller University Press 1978-11-01 /pmc/articles/PMC2185059/ /pubmed/722239 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 Structural and functional differences between the H-2 controlled Ss and Slp proteins |
title | Structural and functional differences between the H-2 controlled Ss and Slp proteins |
title_full | Structural and functional differences between the H-2 controlled Ss and Slp proteins |
title_fullStr | Structural and functional differences between the H-2 controlled Ss and Slp proteins |
title_full_unstemmed | Structural and functional differences between the H-2 controlled Ss and Slp proteins |
title_short | Structural and functional differences between the H-2 controlled Ss and Slp proteins |
title_sort | structural and functional differences between the h-2 controlled ss and slp proteins |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2185059/ https://www.ncbi.nlm.nih.gov/pubmed/722239 |