Multiple forms of acetylcholinesterase from rat erythrocytes. Effect of fat-free diet.
Electrophoretic patterns of acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) from rat erythrocyte were studied. The enzyme was solubilized by the following treatments: a) Triton X-100, b) sodium deoxycholate, or c) ultrasonic irradiation. When the erythrocyte membrane was solubilized by Triton X-100 at concentrations higher than 0.3%, by 10 mM sodium deoxycholate, or by ultrasonic irradiation for more than 5 min, a single band of acetylcholinesterase activity appeared in the gel. Two bands of activity were stained in the gel when the membrane was solubilized by Triton X-100 at concentrations between 0.1--0.2%, or by ultrasound for 5 min. Electrophoretic patterns of acetylcholinesterase from rats fed a fat-sufficient diet were similar to those for the enzyme from animals fed a fat-free diet. The recombination of lipids with the enzyme eluted from the gels confirmed the "phenotypic allosteric desensitization phenomenon".
D000110:Acetylcholinesterase / Q000097:blood* / Q000302:isolation & purification; D000818:Animals; D001665:Binding Sites; D003840:Deoxycholic Acid; D004041:Dietary Fats; D004912:Erythrocytes / Q000187:drug effects / Q000201:enzymology*; D005459:Fluorides / Q000494:pharmacology; D007527:Isoenzymes / Q000097:blood*; D008055:Lipids / Q000097:blood; D011485:Protein Binding; D051381:Rats; D012995:Solubility; D014465:Ultrasonics
D004041:Dietary Fats; D007527:Isoenzymes; D008055:Lipids; D003840:Deoxycholic Acid; D000110:Acetylcholinesterase; D005459:Fluorides