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. 1987 Jan 15;241(2):615–619. doi: 10.1042/bj2410615

Removal of covalently bound inositol from Torpedo acetylcholinesterase and mammalian alkaline phosphatases by deamination with nitrous acid. Evidence for a common membrane-anchoring structure.

M G Low, A H Futerman, K E Ackermann, W R Sherman, I Silman
PMCID: PMC1147604  PMID: 3593210

Abstract

Our earlier evidence suggested that both acetylcholinesterase and alkaline phosphatase are anchored to the cell surface via covalently-attached phosphatidylinositol [Low, Futerman, Ferguson & Silman (1986) Trends Biochem. Sci. 11, 212-215]. We now present chemical data, based upon a nitrous acid deamination reaction, showing that in both proteins the phosphatidylinositol moiety is attached through a glycosidic linkage to a sugar residue bearing a free amino group.

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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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