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

Biochem J. 1987 Jan 15;241(2):615-9. doi: 10.1042/bj2410615.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylcholinesterase / metabolism*
  • Alkaline Phosphatase / metabolism*
  • Animals
  • Cattle
  • Cell Membrane / enzymology
  • Deamination
  • Humans
  • Inositol / analysis*
  • Nitrites / pharmacology*
  • Nitrous Acid / pharmacology*
  • Protein Binding
  • Torpedo

Substances

  • Nitrites
  • Inositol
  • Acetylcholinesterase
  • Alkaline Phosphatase
  • Nitrous Acid