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

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.

authors

Roberts WL,Rosenberry TL

doi

10.1016/0006-291x(85)90950-7

subject

Has Abstract

pub_date

1985-12-17 00:00:00

pages

621-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(85)90950-7

journal_volume

133

pub_type

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