Abstract
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.
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