Abstract
Abstract A lymphoid-cell specific surface membrane antigen of the mouse has been purified over 200-fold by differential solubilization, ion exchange chromatography and gel filtration. The serologic activity corresponded to a fraction of 67,000 molecular weight. Two main protein bands could be detected in acrylamide gel electrophoresis together with a very faint third band. Double gel diffusion revealed a single strong band of precipitation, whereas no immunoprecipitation could be detected in conventional—or crossing-over immunoelectrophoresis. This discrepancy is discussed. The antigen was strongly expressed on cells having an organ distribution similar to bone marrow-derived cells and slightly expressed on a subpopulation of cells which was similarly abundant in all lymphoid organs tested. During ontogeny the antigen was strongly expressed on thymocytes with a transient maximum between days 4 and 8 after gestation.
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