The organization of the transforming protein encoded by Abelson murine leukemia virus (A-MuLV) in transformed lymphoid and fibroblast cells was examined using immunofluorescent analysis. Antibodies specific for v-abl were capable of detecting cytoplasmic Abelson protein molecules in fixed cells, but none were able to stain the surface of live A-MuLV transformed cells. However, a series of monoclonal antibodies selected for the ability to bind to the surface of A-MuLV-transformed cells did stain live cells. These antibodies were shown to react with a determinant within the helper virus-derived p15 sequences that are present at the amino terminus of the Abelson protein, indicating that gag-derived determinants are exposed on the surface of transformed cells. The inability of a p12-specific monoclonal antibody to stain live cells indicates that only a small portion of the amino terminal sequences are exposed. Examination of the ability of these antibodies to react with Abelson protein encoded by a series of gag deletion mutants suggests that the determinant recognized by these antibodies lies between amino acids 38 and 114 of p15.