Relationship between adenosine deaminase and a human thymus leukemia antigen isolated from MOLT 4 cells.
The relationship between adenosine deaminase (ADA) and a human membrane thymus leukemia (HTL) antigen-detected by an antithymocyte serum was explored. A freeze-thaw extract of the T-cell-derived cell line, MOLT 4, was applied to an immunoabsorbant column of a rabbit antiserum to calf ADA. The bound MOLT 4 ADA was eluted with 6 M urea. The recovered ADA had a specific activity of 490 mumol of adenosine deaminated per min per mg protein, and the yield was 32%. No HTL antigenic activity was detected in the purified ADA. In addition, no ADA activity was detected in the unbound fraction containing the HTL antigenic activity, supporting the conclusion that ADA and HTL antigen are independent molecules. Affinity-purified anti-calf ADA was not cytotoxic for several HTL antigen-positive cells, including thymocytes, MOLT 4, and thymus-derived acute leukemia lymphoblasts.
D000243:Adenosine Deaminase / Q000032:analysis*; D000818:Animals; D000912:Antibodies, Neoplasm; D000951:Antigens, Neoplasm / Q000032:analysis*; D006801:Humans; D007527:Isoenzymes / Q000032:analysis; D007942:Leukemia, Experimental / Q000032:analysis* / Q000201:enzymology; D008214:Lymphocytes / Q000276:immunology; D008565:Membrane Proteins / Q000032:analysis; D009700:Nucleoside Deaminases / Q000032:analysis*
D000912:Antibodies, Neoplasm; D000951:Antigens, Neoplasm; D007527:Isoenzymes; D008565:Membrane Proteins; D009700:Nucleoside Deaminases; D000243:Adenosine Deaminase