Removal of covalently bound inositol from Torpedo acetylcholinesterase and mammalian alkaline phosphatases by deamination with nitrous acid. Evidence for a common membrane-anchoring structure.
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.
D000110:Acetylcholinesterase / Q000378:metabolism*; D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology; D003641:Deamination; D006801:Humans; D007294:Inositol / Q000032:analysis*; D009573:Nitrites / Q000494:pharmacology*; D009608:Nitrous Acid / Q000494:pharmacology*; D011485:Protein Binding; D014101:Torpedo
D009573:Nitrites; D007294:Inositol; D000110:Acetylcholinesterase; D000469:Alkaline Phosphatase; D009608:Nitrous Acid