[Purification of the acetylcholinesterase from human erythrocytes by affinity chromatography (author's transl)].
The acetylcholinesterase from human erythrocytes was released from the plasma membrane with 0.2% Triton X-100 at low ionic strength and purified by two affinity chromatography steps on Sepharose-bound m-[6-(6-amino-caproylamino)caproylamino]phenyltrimethyl-ammonium. The synthesis of the inhibitor is described. The purified, detergent-free acetylcholinesterase was obtained with a specific activity of 4270 U/mg (158000-fold purification) and a 28% yield. The enzyme is a glycoprotein and aggregates in the absence of Triton X-100 into higher molecular complexes. The molecular weight was estimated by sodium dodecylsulfate electrophoresis to be 80000 +/- 3000 in the presence of 2-mercapto-ethanol and 154000 +/- 6000 in its absence.
D000110:Acetylcholinesterase / Q000097:blood* / Q000302:isolation & purification; D002462:Cell Membrane / Q000201:enzymology; D002800:Cholinesterase Inhibitors; D002846:Chromatography, Affinity; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D046911:Macromolecular Substances; D008970:Molecular Weight; D011092:Polyethylene Glycols; D000644:Quaternary Ammonium Compounds / Q000138:chemical synthesis / Q000494:pharmacology
D002800:Cholinesterase Inhibitors; D046911:Macromolecular Substances; D000644:Quaternary Ammonium Compounds; D011092:Polyethylene Glycols; D000110:Acetylcholinesterase
Affinitätschromatographische Reinigung der Acetylcholinesterase aus menschlichen Erythrozyten