Abstract
THE important role of mammalian tyrosinase in the formation of melanin has been convincingly demonstrated1. In all earlier studies, tyrosine has been thought to be the only effective substrate, with the exception of tyrosine ethyl ester which was found by Lerner et al.2 to be oxidized by Harding–Passey melanoma tyrosinase preparations. In a few cases, tyrosine peptides have been investigated as potential substrates, and Bloch3 found that human skin extracts could not oxidize glycyl-dihydroxyphenyl-alanine, while Kertész4 reported that glycyl-L-tyrosine was not oxidized by tyrosinase preparations obtained from human melanomas. Lerner1 predicted that tyrosine peptides in which tyrosine occupies the N-terminal position would be substrates of mammalian tyrosinase, but that tyrosine peptides in which tyrosine occupied the C-terminal position would not.
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References
Lerner, A. B., “Advances in Enzymology”, 14, 86 (1953).
Lerner, A. B., Fitzpatrick, T. B., Calkins, E., and Summerson, W. H., J. Biol. Chem., 191, 799 (1951).
Bloch, Bruno, in Jadassohn, J., “Handbuch der Haut- und Gteschlectskrankheiten”, 1, 434 (1927).
Kertész, D., J. Nat. Cancer Inst., 14, 1081 (1954).
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YASUNOBU, K. Tyrosine Peptides as Precursors of Melanin in Mammals. Nature 180, 441–442 (1957). https://doi.org/10.1038/180441a0
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DOI: https://doi.org/10.1038/180441a0
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