Paper Report for: Frenkel_1980_Eur.J.Biochem_109_377
Reference
Title: Lipid-protein interactions in human erythrocyte-membrane acetylcholinesterase. Modulation of enzyme activity by lipids Frenkel EJ, Roelofsen B, Brodbeck U, van Deenen LL, Ott P Ref: European Journal of Biochemistry, 109:377, 1980 : PubMed
Purified human erythrocyte membrane acetylcholinesterase was incorporated into vesicles of various lipid compositions. The activities of the free and the lipid-associated enzyme were assayed at temperatures between 4 degrees C and 40 degrees C and the results were visualized as plots of log v versus 1/T (Arrhenius plots). For the purified, detergent-depleted enzyme a linear relation was obtained. If Triton X-100 was added to the assay medium a curved plot resulted. For acetylcholinesterase incorporated into dimyristoylphosphatidylcholine vesicles a clear break in the plot was observed at the phase transition temperature of the lipid. With lipids not experiencing a phase transition within the temperature range investigated, again a linear relation was obtained. These results show that the activity of human erythrocyte membrane acetylcholinesterase is strongly modulated by its hydrophobic environment.
        
Related information
Citations formats
Frenkel EJ, Roelofsen B, Brodbeck U, van Deenen LL, Ott P (1980) Lipid-protein interactions in human erythrocyte-membrane acetylcholinesterase. Modulation of enzyme activity by lipids European Journal of Biochemistry109: 377-82
Frenkel EJ, Roelofsen B, Brodbeck U, van Deenen LL, Ott P (1980) European Journal of Biochemistry109: 377-82