Solubilization and biochemical characterization of the melatonin deacetylase from Xenopus laevis retina.

@article{Grace1993SolubilizationAB,
  title={Solubilization and biochemical characterization of the melatonin deacetylase from Xenopus laevis retina.},
  author={Michael S. Grace and Joseph C Besharse},
  journal={Journal of neurochemistry},
  year={1993},
  volume={60 3},
  pages={
          990-9
        }
}
Melatonin deacetylase, an enzyme activity recently discovered in the Xenopus laevis retina, regulates local melatonin levels. The deacetylase occurs in retina, retinal pigment epithelium, and skin, all sites of melatonin action, and is widely distributed among vertebrates. We have solubilized the enzyme from Xenopus retina and pigment epithelium using nonionic detergents, and have developed a specific enzyme assay. We have characterized the enzyme and now report that the deacetylase is… CONTINUE READING