Abstract
p97 is a 97,000-molecular weight (MW) cell-surface glyco-protein, which is present in most human melanomas but in only trace amounts in normal tissues1–4. We describe here the purification of p97 by affinity chromatography with monoclonal antibody, followed by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), and determination of the N-terminal amino acid sequence using a new, highly sensitive protein sequencer5. The sequence was found to be homologous to the N-terminal sequences of transferrin and lactotransferrin. This structural homology was confirmed by the observation that antiserum to denatured p97 cross-reacted with denatured transferrin and lactotransferrin. We have also demonstrated that p97 is functionally related to transferrin and lactotransferrin in that it binds iron. This is one of the first reports of the amino acid sequence of a human tumour-associated cell-surface antigen and one of the few cases in which insight has been obtained into its function.
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Brown, J., Hewick, R., Hellström, I. et al. Human melanoma-associated antigen p97 is structurally and functionally related to transferrin. Nature 296, 171–173 (1982). https://doi.org/10.1038/296171a0
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DOI: https://doi.org/10.1038/296171a0
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