Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure

J. D. Capra, E. S. Vitetta, J. Klein

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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 sulfatepolyacrylamide 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 β2 microglobulin.

Original languageEnglish (US)
Pages (from-to)664-672
Number of pages9
JournalJournal of Experimental Medicine
Volume142
Issue number3
DOIs
StatePublished - Jan 1 1975

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Molecular Weight
Disulfides
Immune Sera
Proteins
Gels
Sodium
Carbohydrates

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology

Cite this

Capra, J. D. ; Vitetta, E. S. ; Klein, J. / Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure. In: Journal of Experimental Medicine. 1975 ; Vol. 142, No. 3. pp. 664-672.
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Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure. / Capra, J. D.; Vitetta, E. S.; Klein, J.

In: Journal of Experimental Medicine, Vol. 142, No. 3, 01.01.1975, p. 664-672.

Research output: Contribution to journalArticle

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