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Immunoaffinity chromatography of a cellular tumor antigen from mouse neuroblastoma cells
Author(s) -
Levitsky Kenneth,
Chandrasekaran Krish,
Mora Peter T.,
Simmons Daniel T.
Publication year - 1983
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910320513
Subject(s) - neuroblastoma , monoclonal antibody , sedimentation coefficient , microbiology and biotechnology , antigen , affinity chromatography , biology , methionine , tumor cells , antibody , chemistry , biochemistry , cell culture , cancer research , amino acid , immunology , enzyme , genetics
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.