Structural analysis of thymus-leukemia (TL) antigens in the mouse

K. R. McIntyre, U. Hammerling, J. W. Uhr, E. S. Vitetta

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11 Scopus citations

Abstract

Thymus-leukemia (TL) antigens have been sequentially immunoprecipitated from glycoprotein pools prepared from lysates of biosynthetically labeled ASL-1w leukemia cells with a monoclonal antibody and a standard alloantiserum. Results suggest that on leukemia cells from Tla(a) mice, as previously reported for thymocytes from these mice, all the alloantiserum-defined TL specificities (TL.1, 2, 3, 5, 6) as well as the specificity defined by the monoclonal antibody (TL.m3) are carried by a single molecular species. The degree of structural homology between the 45,000-m.w. heavy chains of TL and H-2 was investigated by the technique of comparative tryptic peptide mapping. Results indicate that TL is more distantly related at the primary structural level to H-2 than H-2 antigens are to one another.

Original languageEnglish (US)
Pages (from-to)1712-1717
Number of pages6
JournalJournal of Immunology
Volume128
Issue number4
StatePublished - 1982

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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    McIntyre, K. R., Hammerling, U., Uhr, J. W., & Vitetta, E. S. (1982). Structural analysis of thymus-leukemia (TL) antigens in the mouse. Journal of Immunology, 128(4), 1712-1717.