Your browser version may not work well with NCBI's Web applications. More information here...
1: Pigment Cell Res. 1992 Oct;5(4):162-7.Links

Isolation and characterization of a chicken tyrosinase cDNA.

Mochii M, Iio A, Yamamoto H, Takeuchi T, Eguchi G.

Department of Developmental Biology, National Institute for Basic Biology, Okazaki, Japan.

Complementary DNA clones coding for chicken tyrosinase were isolated from retinal pigmented epithelium of chicken embryo. Sequence analysis shows that one of the cDNA clones consisting of 1,997 nucleotides has an open reading frame coding for 529 amino acids. The deduced protein has nine N-glycosylation sites and a transmembrane region. A sequence comparison of the deduced chicken tyrosinase with the mouse and human homologues revealed that amino acid sequences are conserved for the entire polypeptides. Seventy-two percent and 73% of amino acids in the chicken sequence are identical to that of the mouse and human tyrosinases, respectively. Histidines neighboring the postulated copper-binding sites and the cysteines are well conserved. RNA blotting analysis showed that a major transcript of 2.5 kb is detected in retinal pigmented epithelium of a 9-day-old chicken embryo.

PMID: 1494538 [PubMed - indexed for MEDLINE]