Acetylcholinesterase and Its Association with Lipid
Open Access
- 1 April 1976
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 63 (2), 519-524
- https://doi.org/10.1111/j.1432-1033.1976.tb10255.x
Abstract
Human erythrocyte acetylcholinesterase preparations which vary in lipid content, from lipid-rich to lipid-poor, have been successfully prepared using deoxycholate. It was found that the lipid content of the enzyme decreased gradually as the deoxycholate concentration used in its preparation was increased. The binding of lipid to lipid-poor preparations of the enzyme has been investigated. It was found that the activity of such preparations was highly dependent on their phospholipid contents. Maximum specific activity was associated with a fixed phospholipid content. The lipid-poor enzyme was highly activated by addition of either endogenous(membrane) or exogenous lipid. Based on the data presented, it was concluded that acetylcholinesterase is a phospholipoprotein, and its activity is highly dependent on its phospholipid componentKeywords
This publication has 14 references indexed in Scilit:
- A simple method for purification of acetylcholinesterase from human erythrocyte membranesBiochimica et Biophysica Acta (BBA) - Enzymology, 1974
- The Effect of Delipidation on the Adenosine Triphosphatase of Sarcoplasmic Reticulum. Electron Microscopy and Physical PropertiesEuropean Journal of Biochemistry, 1974
- Solubilization and Purification of Human Erythrocyte Membrane AcetylcholinesteraseExperimental Biology and Medicine, 1973
- Localization of red cell membrane constituentsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1973
- Human erythrocyte membrane bound enzyme acetylcholinesteraseBiochimica et Biophysica Acta (BBA) - Biomembranes, 1972
- Acetylcholinesterase Interaction with a Lipoprotein MatrixEuropean Journal of Biochemistry, 1971
- Removal of lipids from human plasma low-density lipoprotein by detergentsBiochemistry, 1971
- Stability of the bovine erythrocyte membrane. Release of enzymes and lipid componentsBiochemistry, 1968
- A new and rapid colorimetric determination of acetylcholinesterase activityBiochemical Pharmacology, 1961
- Purification of human red cell acetylcholinesteraseArchives of Biochemistry and Biophysics, 1954