• DOI:10.1016/s0021-9258(19)69463-9
Corpus ID: 37622735

Retinyl palmitate hydrolase activity in normal rat liver.

@article{Prystowsky1981RetinylPH,
  title={Retinyl palmitate hydrolase activity in normal rat liver.},
  author={J. H. Prystowsky and J. E. Smith and D. S. Goodman},
  journal={The Journal of biological chemistry},
  year={1981},
  volume={256 9},
  pages={
          4498-503
        }
}

J. H. Prystowsky, J. E. Smith, D. S. Goodman

Published 1981

Medicine, Chemistry

The Journal of biological chemistry

Retinyl esters are hydrolyzed in liver both during uptake and mobilization of vitamin A. Studies were conducted to explore the enzymatic hydrolysis of retinyl palmitate in normal rat liver. Retinyl palmitate hydrolase activity was assayed with a sensitive and accurate microassay, employing retinyl [~-‘~C]palmitate as substrate. The products of the reaction were identified as retinol and free fatty acid. Hydrolase activity was stimulated by sodium cholate and inhibited by a-tocopherol… CONTINUE READING

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