Identification of covalently attached fatty acids in the hydrophobic membrane-binding domain of human erythrocyte acetylcholinesterase

William L. Roberts, Terrone L. Rosenberry

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

Human erythrocyte acetylcholinesterase is an amphipathic enzyme whose hydrophobic membrane-binding domain can be selectively labeled with a lipophilic photoreagent and removed by digestion with papain. In this paper we demonstrate that methanolysis releases covalently bound fatty acids from the hydrophobic domain and thus confirm that this domain is a covalently linked glycolipid at the enzyme subunit C-terminus. About one mole of saturated and one mole of unsaturated fatty acids were released per mole of domain. Since the predominant unsaturated fatty acids (22:4 and 22:5) are minor components of the esterified fatty acid pool in human erythrocyte membranes, assembly of the glycolipid must involve a selected unsaturated fatty acid pool.

Original languageEnglish (US)
Pages (from-to)621-627
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume133
Issue number2
DOIs
StatePublished - Dec 17 1985
Externally publishedYes

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Acetylcholinesterase
Unsaturated Fatty Acids
Fatty Acids
Erythrocytes
Glycolipids
Membranes
Papain
Erythrocyte Membrane
Enzymes
Digestion

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Identification of covalently attached fatty acids in the hydrophobic membrane-binding domain of human erythrocyte acetylcholinesterase. / Roberts, William L.; Rosenberry, Terrone L.

In: Biochemical and Biophysical Research Communications, Vol. 133, No. 2, 17.12.1985, p. 621-627.

Research output: Contribution to journalArticle

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