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Updated: Jul 29, 2026

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction
Published on: April 26, 2011
Chemical analysis of lipid-modified membrane proteins in Acholeplasma laidlawii
M Le Hénaff1, A Chollet, C Fontenelle
1UMR CNRS 6026, Groupe Membranes et Osmorégulation, Université de Rennes 1, Campus de Beaulieu, F-35042 Rennes Cedex, France. m-lehenaff@enitab.fr
Abstract:
The lipid modification of membrane proteins was investigated in Acholeplasma laidlawii by metabolic labeling and by chemical analysis. A S-glycerylcysteine residue was identified from membrane proteins and we reported the strong preference for saturated acyl chains into the lipid modification. Differential release of fatty acids revealed a ratio [(O-ester- + amide-bound acyl chains)/O-ester-linked chains] close to 1.1 which suggests the involvement of only two O-ester linked fatty acids in the acylation process. Present data indicate that acyl proteins in A. laidlawii are true lipoproteins (mainly diacylated) probably processed by a mechanism analogous to that described for eubacteria and other mycoplasmas.
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