L-tyrosine-binding proteins on melanoma cells.
Crosslinking of [14C]L-tyrosine to at least five hamster melanoma cell surface proteins is reported. This effect was abolished by addition of nonradioactive L-tyrosine, L-phenylalanine, or L-dopa, but not by D-tyrosine, tyramine, dopamine, norepinephrine, or epinephrine. The above proteins can be purified by tyrosine-affinity chromatography. They have molecular weights different from proteins staining for dopa oxidase and proteins that bind anti-tyrosinase antibody in Western blots. It is suggested that they may be a hithergo unrecognized part of the cellular apparatus governing melanogenesis.
Slominski
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Department of Immunology and Microbiology, Albany Medical College, New York 12208.
D000818:Animals; D000906:Antibodies / Q000276:immunology; D015153:Blotting, Western; D002250:Carbon Radioisotopes; D002846:Chromatography, Affinity; D006224:Cricetinae; D007980:Levodopa / Q000032:analysis / Q000378:metabolism / Q000494:pharmacology; D008545:Melanoma / Q000378:metabolism* / Q000473:pathology; D008970:Molecular Weight; D014442:Monophenol Monooxygenase / Q000032:analysis / Q000378:metabolism; D010649:Phenylalanine / Q000032:analysis / Q000378:metabolism / Q000494:pharmacology; D011485:Protein Binding; D014407:Tumor Cells, Cultured / Q000378:metabolism / Q000473:pathology; D014443:Tyrosine / Q000276:immunology / Q000378:metabolism*
D000906:Antibodies; D002250:Carbon Radioisotopes; D014443:Tyrosine; D007980:Levodopa; D010649:Phenylalanine; D014442:Monophenol Monooxygenase