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. 1995 Feb 28;92(5):1550–1554. doi: 10.1073/pnas.92.5.1550

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

S E Maxwell 1, S Ramalingam 1, L D Gerber 1, S Udenfriend 1
PMCID: PMC42557  PMID: 7878018

Abstract

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-placental alkaline phosphatase are the amounts of GPI in the cells and the amino acid substituent at the omega site of the nascent protein. A mechanism for explaining cleavage both with and without GPI addition is presented, which supports a transamidase type of enzyme as the catalyst.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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