Di Francesco_1981_Biochim.Biophys.Acta_640_359

Reference

Title : Interaction of human red cell membrane acetylcholinesterase with phospholipids - Di Francesco_1981_Biochim.Biophys.Acta_640_359
Author(s) : Di Francesco C , Brodbeck U
Ref : Biochimica & Biophysica Acta , 640 :359 , 1981
Abstract :

Liposomes of phospholipids fully sustain the enzyme activity of the amphiphile-dependent dimers of human erythrocyte membrane acetylcholinesterase; no head group specificity exists. Diacylglycerides, glycerophosphorylcholine, or free fatty acids do not sustain the catalytic activity. It could be shown that the dimeric acetylcholinesterase with an exposed hydrophobic region can penetrate the lipid bilayer of liposomes and thus becomes stabilized by the surrounding phospholipid molecules.

PubMedSearch : Di Francesco_1981_Biochim.Biophys.Acta_640_359
PubMedID: 7213691

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Citations formats

Di Francesco C, Brodbeck U (1981)
Interaction of human red cell membrane acetylcholinesterase with phospholipids
Biochimica & Biophysica Acta 640 :359

Di Francesco C, Brodbeck U (1981)
Biochimica & Biophysica Acta 640 :359