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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 |
| Sumario: | 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. |
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