Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Extraction of membrane proteins from erythrocytes into sonicated phosphatidylcholine vesicles is described. In a process involving phospholipid and neutral lipid exchange, cell membrane proteins associate with the vesicles and can be separated from the cells by centrifugation. The protein transfer appears to be reversible; phospholipid vesicles mediate the delivery of small amounts of previously extracted protein into cell membranes. Prior to extraction, all but one of the proteins are accessible to lactoperoxidase iodination, and lipid analysis indicates that primarily the outer monolayer of the cell is involved in phospholipid exchange. Among the extracted proteins is acetylcholinesterase which is removed much more efficiently by this procedure than by concentrated salt solutions. The most abundant proteins of the erythrocyte membrane are not represented in the vesicle extract.
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PMID:Selective extraction of membrane-bound proteins by phospholipid vesicles. 89 40

1. Crossed immunoelectrophoresis was used for extensive characterization of individual proteins of human erythrocyte membranes solubilized in non-ionic detergent. 2. The precipitates were assigned to extrinsic or intrinsic proteins. 3. Four glycoproteins were identified by their lectin binding behaviour, whilst five proteins were affected by neuraminidase, indicating them to be sialoglycoproteins. 4. Enzymatic activity is retained in the solubilized system and the presence of acetylcholinesterase and an ATPase was demonstrated. The formation of phosphorylated membrane proteins on incubation with [32P]ATP was demonstrated by autoradiography on the immunoelectrophoresis plates. 5. Five proteins located on the outer cell surface were identified by antibody binding to intact cells. These same proteins were degraded by proteolytic enzymes in intact cells but only three of them were labelled by lactoperoxidase-catalysed 125I-iodination. 6. Analysis of erythrocyte membrane proteins using quantitive immunoelectrophoresis yields results concordant with those obtained by dodecyl sulfate-polyacrylamide gel electrophoresis.
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PMID:The immunochemical approach to the characterization of membrane proteins. Human erythrocyte membrane proteins analysed as a model system. 99 Mar 30

Bovine milk lactoperoxidase, eel acetylcholinesterase, and Aeromonas aminopeptidase were photooxidized and inactivated in broad-spectrum visible light in the presence of 2,3-butanedione and 1-phenyl-1,2-propanedione. Methylglyoxal caused similar effects at 254 nm. 2-Thiol-L-histidine and 3-methyl-L-histidine protected the enzymes against photoinactivation more effectively then N3-, even at a molar ratio of 2:1 (protector to enzyme). These compounds also delayed the photoinactivation of acetylcholinesterase, induced by ultraviolet light.
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PMID:Oxidation, photosensitized by certain diketones, of enzymes and protection against such oxidation by histidine derivatives. 706 88