Immunoaffinity chromatography of a cellular tumor antigen from mouse neuroblastoma cells.
The cellular tumor antigen p53 was isolated from mouse neuroblastoma cells and was found in a form not complexed to another protein. The p53 in these cells was stable, turning over about every 10 h. Its methionine-labelled tryptic peptides were very similar to those of the p53 isolated from SV40-transformed mouse cells. The labelled protein was purified from neuroblastoma cells by immunoaffinity using specific monoclonal antibodies and was about 80% radiochemically pure. Furthermore, the purified p53 sedimented in sucrose gradients with a sedimentation coefficient of approximately 8S. This correlated with the sedimentation coefficient of p53 prior to purification, showing that the purified protein retained its native size.
D000818:Animals; D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm / Q000302:isolation & purification*; D002460:Cell Line; D002499:Centrifugation, Density Gradient; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006207:Half-Life; D051379:Mice; D009363:Neoplasm Proteins / Q000302:isolation & purification*; D009447:Neuroblastoma / Q000276:immunology*; D010750:Phosphoproteins / Q000302:isolation & purification*; D016159:Tumor Suppressor Protein p53; D014412:Tumor Virus Infections
D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm; D009363:Neoplasm Proteins; D010750:Phosphoproteins; D016159:Tumor Suppressor Protein p53