Characterization of lipid–protein interactions in acetylcholinesterase lipoprotein extracted from bovine erythrocytes
- 1 April 1979
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 179 (1), 109-117
- https://doi.org/10.1042/bj1790109
Abstract
Acetylcholinesterase was released from bovine erythrocytes in hypo-osmotic sodium phosphate buffer. Initially, about 30% of the enzyme was released in a soluble lipoprotein form, and further incubation resulted in the progressive release of the enzyme in a particulate form. Solubilization of the acetylcholinesterase in the particulate fraction with Lubrol WX (2 mg/ml) resulted in the loss of all lipids except a non-exchangeable fraction identified as cardiolipin. Addition of a mixture of erythrocyte phospholipids to the soluble forms and to the Lubrol WX-solubilized enzyme resulted in the formation of particulate forms of the enzyme with increased partial specific volume and Stokes radius, and a break in the Arrhenius plot of the enzyme activity around 20 degrees C. The break in the Arrhenius plot was abolished by treatment of a soluble enzyme preparation with 1.8 M salt (NaCl) in phosphate buffer, conditions that allowed the extraction of cardiolipin from the enzyme by chloroform/methanol. Failure of the high-salt treatment to decrease the Stokes radius made it unlikely that the bound cardiolipin formed a boundary layer or annulus around the protein. It is suggested that cardiolipin is bound to the core of the dimeric protein structure, thereby controlling the acetylcholinesterase activity.This publication has 31 references indexed in Scilit:
- Interactions of acetylcholine receptor and acetylcholinesterase with lipid monolayersBiochimica et Biophysica Acta (BBA) - Biomembranes, 1978
- Lipid requirements for cytochrome c oxidase activityBiochemistry, 1977
- Non‐lytic release of acetylcholinesterase from erythrocytes by A phosphatidylinositol‐specific phospholipase CFEBS Letters, 1977
- Selective extraction of membrane-bound proteins by phospholipid vesicles.Journal of Biological Chemistry, 1977
- Studies on the characterization of human erythrocyte acetylcholinesterase and its interaction with antibodiesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1977
- Acetylcholinesterase Inactivation of Enzymetreated ErythrocytesNature, 1963
- THE EFFECTS OF TRYPSIN AND CHYMOTRYPSIN ON THE ACETYLCHOLINESTERASE CONTENT OF HUMAN ERYTHROCYTESAustralasian Annals of Medicine, 1963
- A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein MixturesJournal of Biological Chemistry, 1961
- STUDIES OF THE LIPIDS OF THE ERYTHROCYTE .1. QUANTITATIVE ANALYSIS OF THE LIPIDS OF NORMAL HUMAN RED BLOOD CELLS1960
- A SPECTROPHOTOMETRIC METHOD FOR MEASURING THE BREAKDOWN OF HYDROGEN PEROXIDE BY CATALASEJournal of Biological Chemistry, 1952