In vivo regulation of phenylalanine hydroxylation to tyrosine, studied using enrichment in apoB-100.

@article{Rafii2008InVR,
  title={In vivo regulation of phenylalanine hydroxylation to tyrosine, studied using enrichment in apoB-100.},
  author={Mahroukh Rafii and Jane M McKenzie and Susan A Roberts and George Steiner and Ronald O. Ball and Paul B. Pencharz},
  journal={American journal of physiology. Endocrinology and metabolism},
  year={2008},
  volume={294 2},
  pages={E475-9}
}
Phenylalanine hydroxylation is necessary for the conversion of phenylalanine to tyrosine and disposal of excess phenylalanine. Studies of in vivo regulation of phenylalanine hydroxylation suffer from the lack of a method to determine intrahepatocyte enrichment of phenylalanine and tyrosine. apoB-100, a hepatic export protein, is synthesized from intrahepatocyte amino acids. We designed an in vivo multi-isotope study, [(15)N]phenylalanine and [2H2]tyrosine to determine rates of phenylalanine… CONTINUE READING