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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antibodies / immunology
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Blotting, Western
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Carbon Radioisotopes
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Chromatography, Affinity
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Cricetinae
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Levodopa / analysis
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Levodopa / metabolism
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Levodopa / pharmacology
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Melanoma / metabolism*
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Melanoma / pathology
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Molecular Weight
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Monophenol Monooxygenase / analysis
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Monophenol Monooxygenase / metabolism
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Phenylalanine / analysis
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Phenylalanine / metabolism
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Phenylalanine / pharmacology
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Protein Binding
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Tumor Cells, Cultured / metabolism
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Tumor Cells, Cultured / pathology
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Tyrosine / immunology
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Tyrosine / metabolism*
Substances
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Antibodies
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Carbon Radioisotopes
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Tyrosine
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Levodopa
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Phenylalanine
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Monophenol Monooxygenase