Purification and partial amino acid sequence analysis of the cellular tumour antigen, p53, from mouse SV40-transformed cells.

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Abstract
The cellular tumor antigen p53 is implicated in the transformation process. To compare p53 from transformed cells and their normal counterparts in detail, and so to identify any structural differences that might alter p53 function, requires information on the primary structure of the protein. By making use of immunochemical techniques it was possible to purify nanomole amounts of p53. This was sufficient, using high sensitivity automated gas-phase sequencing techniques to determine the amino acid sequence of 2 tryptic peptides from p53. Their sequences agree completely with the predicted polypeptide sequence derived from a cloned c[complementary]DNA for p53 mRNA and provide the first data on the amino acid sequence of p53. A combination of the high sensitivity amino acid sequencing procedures used here and cDNA sequence analysis should provide the complete amino acid sequence of p53.