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Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure
The murine Ss protein has been isolated and purified. Using specific antisera, the radiolabeled protein has a mol wt of 120,000 in sodium dodecyl sulfate polyacrylamide gels. It is composed of two basic subunits of 23,000 and 14,000 daltons. The smaller molecular weight subunit contains a single dis...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1975
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189919/ https://www.ncbi.nlm.nih.gov/pubmed/809530 |
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collection | PubMed |
description | The murine Ss protein has been isolated and purified. Using specific antisera, the radiolabeled protein has a mol wt of 120,000 in sodium dodecyl sulfate polyacrylamide gels. It is composed of two basic subunits of 23,000 and 14,000 daltons. The smaller molecular weight subunit contains a single disulfide bridge, is devoid of carbohydrate, and may represent the murine equivalent of beta2-microglobulin. |
format | Text |
id | pubmed-2189919 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1975 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21899192008-04-17 Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure J Exp Med Articles The murine Ss protein has been isolated and purified. Using specific antisera, the radiolabeled protein has a mol wt of 120,000 in sodium dodecyl sulfate polyacrylamide gels. It is composed of two basic subunits of 23,000 and 14,000 daltons. The smaller molecular weight subunit contains a single disulfide bridge, is devoid of carbohydrate, and may represent the murine equivalent of beta2-microglobulin. The Rockefeller University Press 1975-09-01 /pmc/articles/PMC2189919/ /pubmed/809530 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 Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure |
title | Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure |
title_full | Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure |
title_fullStr | Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure |
title_full_unstemmed | Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure |
title_short | Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure |
title_sort | studies on the murine ss protein. i. purification, molecular weight, and subunit structure |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189919/ https://www.ncbi.nlm.nih.gov/pubmed/809530 |