
Tumor-specific transplantation antigen (TSTA) activity was investigated (with the use of inbred BALB/c and C3H mice and inbred Fisher and Wistar rats) in various early polyomavirus (Py)-coded proteins by three methodologies: 1) immunoprecipitation by anti-T-antigen sera, gel slicing, and immunization; 2) affinity chromatography with the use of anti-tumor-associated antigen serum; and 3) use of a Py mutant, NG18. The results obtained by all three techniques allowed refutation of the hypothesis that the three major species of T-antigen possess the main TSTA activity, particularly middle-sized T-antigen which is a plasma membrane protein. TSTA activity was found to be associated with proteins having a molecular weight of approximately 37,000. The exact origin of this protein is discussed.
Mice, Inbred BALB C, Mice, Inbred C3H, Rats, Inbred Strains, Cell Transformation, Viral, Rats, Molecular Weight, Mice, Antigens, Neoplasm, Mutation, Animals, Polyomavirus, Cells, Cultured
Mice, Inbred BALB C, Mice, Inbred C3H, Rats, Inbred Strains, Cell Transformation, Viral, Rats, Molecular Weight, Mice, Antigens, Neoplasm, Mutation, Animals, Polyomavirus, Cells, Cultured
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