Additional N-glycosylation and its impact on the folding of intestinal lactase-phlorizin hydrolase.

@article{Jacob2000AdditionalNA,
  title={Additional N-glycosylation and its impact on the folding of intestinal lactase-phlorizin hydrolase.},
  author={Ralf Jacob and Jeffrey R Weiner and S Stadge and Hassan Y Naim},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 14},
  pages={10630-7}
}
Lactase-phlorizin hydrolase (LPH) is a membrane bound intestinal hydrolase, with an extracellular domain comprising 4 homologous regions. LPH is synthesized as a large polypeptide precursor, pro-LPH, that undergoes several intra- and extracellular proteolytic steps to generate the final brush-border membrane form LPHbeta(final). Pro-LPH is associated through homologous domain IV with the membrane through a transmembrane domain. A truncation of 236 amino acids at the COOH terminus of domain IV… CONTINUE READING