N-linked glycosylation of the thyroid Na+/I- symporter (NIS). Implications for its secondary structure model.

@article{Levy1998NlinkedGO,
  title={N-linked glycosylation of the thyroid Na+/I- symporter (NIS). Implications for its secondary structure model.},
  author={Ofer Levy and Antonio De la Vieja and Christopher S. Ginter and Claudia Riedel and Guixiang Dai and Nancy Carrasco},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 35},
  pages={22657-63}
}
The Na+/I- symporter (NIS), a 618-amino acid membrane glycoprotein that catalyzes the active accumulation of I- into thyroid cells, was identified and characterized at the molecular level in our laboratory (Dai, G., Levy, O., and Carrasco, N. (1996) Nature 379, 458-460). Because mature NIS is highly glycosylated, it migrates in SDS-polyacrylamide gel electrophoresis as a broad polypeptide of higher molecular mass (approximately 90-110 kDa) than nonglycosylated NIS (approximately 50 kDa). Using… CONTINUE READING