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

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 Tlaa 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.

• Authors: K R McIntyre, U Hämmerling, J W Uhr, E S Vitetta
• Journal: Journal of immunology (Baltimore, Md. : 1950) (J Immunol) Vol. 128 Issue 4 Pg. 1712-7 (Apr 1982) ISSN: 0022-1767 [Print] United States
• PMID: 7061847 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Antigens, Neoplasm
• Glycoproteins
• H-2 Antigens
• Membrane Glycoproteins
• Peptides
• thymus-leukemia antigens

Topics

• Amino Acid Sequence
• Animals
• Antigens, Neoplasm
• Chemical Precipitation
• Glycoproteins (immunology)
• H-2 Antigens
• Leukemia, Experimental (immunology)
• Membrane Glycoproteins
• Mice
• Mice, Inbred A
• Mice, Inbred BALB C
• Mice, Nude
• Peptides (metabolism)
• Thymus Gland (immunology)