Mutational analysis of the C-terminal signal peptide of bovine liver 5'-nucleotidase for GPI anchoring: a study on the significance of the hydrophilic spacer region.

@article{Furukawa1997MutationalAO,
  title={Mutational analysis of the C-terminal signal peptide of bovine liver 5'-nucleotidase for GPI anchoring: a study on the significance of the hydrophilic spacer region.},
  author={Yoko Furukawa and Kentaro Tsukamoto and Hiroyoshi Ikezawa},
  journal={Biochimica et biophysica acta},
  year={1997},
  volume={1328 2},
  pages={
          185-96
        }
}
Bovine liver 5'-nucleotidase is a GPI-anchored protein whose Ser523 attaches to GPI as the omega-site. For GPI-modification, pro-protein of the enzyme possesses a signal peptide at the C-terminus, comprising a hydrophilic spacer sequence of 8 amino acid residues and the following hydrophobic region of 17 amino acid residues. The C-terminal signal peptide is replaced by GPI on a luminal leaflet of endoplasmic reticulum. To characterize the C-terminal signal peptide for GPI modification, we… CONTINUE READING
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