Corpus ID: 12915955

Tyrosinase activity in the medium of human melanoma cell cultures.

@article{Jergil1983TyrosinaseAI,
  title={Tyrosinase activity in the medium of human melanoma cell cultures.},
  author={Bengt Jergil and Christer Lindbladh and Hans Rorsman and Evald Rosengren},
  journal={Acta dermato-venereologica},
  year={1983},
  volume={63 3},
  pages={
          205-8
        }
}
The medium of cultured melanoma cells was studied for tyrosine hydroxylation and dopa-oxidizing activity. The supernatant obtained after centrifugation at 100 000 g for 2 hours was treated with ammonium sulphate, and the precipitate obtained between 35 and 50% saturation was used. Dopa was determined as the product of tyrosine hydroxylation and 5-S-cysteinyldopa as the product of dopa oxidase activity. Determinations were performed with HPLC and electrochemical detection. Our preparation of… Expand
Enzymatic 5-hydroxylation of L-dopa by a tyrosinase isolated from the sea anemone Metridium senile.
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A particulate tyrosinase has been extracted and purified from tentacles of the sea anemone Metridium senile and catalyzed three different reactions: oxidation of catechols, hydroxylation of L-tyrosine with L-dopa as cofactor and 5-hydroxylations of L.dopa. Expand
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The identification of 5-S-cysteinyldopa as the source of formaldehyde-induced fluorescence of normal and pathological melanocytes started a series of investigations into this amino acid, enzymatic and non-enzymatic oxidation of catecholic compounds and the metabolism of thiols. Expand
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Abstract Among tryptophan metabolites, 3-hydroxykynurenine and 3-hydroxyanthranilic acid are unique because of their o -aminophenolic structures. Therefore, they share a typical chemical behaviourExpand