The temperature-dependence of human erythrocyte acetylcholinesterase activity is not affected by membrane cholesterol enrichment.
The temperature-dependence of both the lipid order parameter (SDPH) and acetylcholinesterase (AChE) activity from native and cholesterol-enriched human erythrocyte membranes was investigated. Cholesterol enrichment abolishes an inflection observed around 30 degrees C in the temperature-dependence of native membrane lipid order parameter, whereas the Arrhenius plot of the enzymic activity is substantially unaffected. These results support the view that the breaks in the Arrhenius plot of the enzyme activity are not related to sudden changes of bulk membrane physical state, but arise from a direct effect of temperature on enzyme conformation.
Spinedi
A
A
Department of Biology, University of Rome, Tor Vergata, Italy.
Rufini
S
S
Luly
P
P
Farias
R N
RN
D000110:Acetylcholinesterase / Q000097:blood*; D002784:Cholesterol / Q000494:pharmacology*; D003902:Detergents / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000201:enzymology*; D005260:Female; D006801:Humans; D007700:Kinetics; D008055:Lipids / Q000097:blood; D008297:Male; D017830:Octoxynol; D011092:Polyethylene Glycols / Q000494:pharmacology; D013696:Temperature
D003902:Detergents; D008055:Lipids; D011092:Polyethylene Glycols; D017830:Octoxynol; D002784:Cholesterol; D000110:Acetylcholinesterase