Arrhenius plots of acetylcholinesterase activity in mammalian erythrocytes and in Torpedo electric organ. Effect of solubilization by proteinases and by a phosphatidylinositol-specific phospholipase C.
The temperature-dependence of the catalytic activity of acetylcholinesterase (AChE) from rat erythrocyte-ghost membranes and from Torpedo electric-organ membranes was examined. In the case of rat erythrocyte AChE, a non-linear Arrhenius plot was observed both before and after solubilization by a phosphatidylinositol-specific phospholipase C or by proteinase treatment. Similarly, no significant differences were observed in Arrhenius plots of Torpedo electric-organ AChE before or after solubilization. These results support our suggestion that the catalytic subunit of AChE does not penetrate deeply into the lipid bilayer of the plasma membrane and also suggest that care must be taken in ascribing break points in Arrhenius plots of membrane-bound enzymes to changes in their lipid environment.
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004557:Electric Organ / Q000201:enzymology*; D010450:Endopeptidases; D004910:Erythrocyte Membrane / Q000201:enzymology*; D007700:Kinetics; D008954:Models, Biological; D051381:Rats; D013696:Temperature; D014101:Torpedo / Q000378:metabolism; D010738:Type C Phospholipases
D000110:Acetylcholinesterase; D010738:Type C Phospholipases; D010450:Endopeptidases