Isolation and characterization of variant cDNAs encoding mouse tyrosinase |
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Authors: | M Terao L Tabe E Garattini D Sartori M Studer B Mintz |
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Affiliation: | Molecular Biology Unit, Istituto di Ricerche Farmacologiche Mario Negri, Milan, Italy. |
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Abstract: | Two different cDNA clones encoding mouse tyrosinase (monophenol oxygenase, E.C. 1.14.18.1) were isolated from B16 melanoma cells, and their primary structure was determined. One of the cDNAs consists of 3309 nucleotides with an open reading frame coding for a peptide of 533 amino acids. The other cDNA is approximately 1600 nucleotides long, with a shorter 3'-untranslated region and a deduced in-frame deletion of 77 amino acid residues with respect to the former clone. Neither of these clones is structurally identical to other described mouse tyrosinase cDNAs (1-3). RNA blotting analysis demonstrates that multiple tyrosinase mRNA species are not only present in B16 melanoma, but also in normal skin melanocytes. |
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