Structural analysis of thymus-leukemia (TL) antigens in the mouse
McIntyre, K.R.; Hämmerling, U.; Uhr, J.W.; Vitetta, E.S.
Journal of Immunology 128(4): 1712-1717
1982
ISSN/ISBN: 0022-1767 PMID: 7061847 Document Number: 195633
Thymus-leukemia (TL) antigens were 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 Tlaa mice, as previously reported for thymocytes from these mice, all the alloantiserum-defined TL specificities (TL.1, 2, 3, 5, 6) and 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 MW H chains of TL and H-2 was investigated by the technique of comparative tryptic peptide mapping. TL appears to be more distantly related at the primary structural level of H-2 than H-2 antigens are to one another.