Cleavage without anchor addition accompanies the processing of a nascent protein to its glycosylphosphatidylinositol-anchored form.

@article{Maxwell1995CleavageWA,
  title={Cleavage without anchor addition accompanies the processing of a nascent protein to its glycosylphosphatidylinositol-anchored form.},
  author={Stephen E. Maxwell and Sandhya Ramalingam and Louise Diekmann Gerber and Sidney Udenfriend},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1995},
  volume={92 5},
  pages={
          1550-4
        }
}
Rough microsomal membranes from most mammalian cells, in the presence of a translation system, process nascent proteins with appropriate COOH-terminal signal peptides to their mature glycosylphosphatidylinositol (GPI)-linked forms. The present study, using preprominiplacental alkaline phosphatase as substrate, shows that as much as 10% of the mature product is cleaved correctly but is not linked to GPI. Some of the factors that influence the relative proportions of GPI linked to free mini… CONTINUE READING

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Cloning of murine glycosyl phosphatidylinositol anchor attachment protein, GPAA1.

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