| pubmed-article:536451 | pubmed:abstractText | The acetylcholinesterase was purified by CM-Sephadex chromatography and affinity chromatography on Sepharose bound m-[6-(6-aminocaproylamino)caproylamino]phenyltrimethylammonium bromide. The purified enzyme was obtained with a specific activity of 5470 U/mg (1160-fold purification) and a 89% yield. The molecular weight of the native enzyme was estimated to be 144,000. The enzyme is split into two subunits of approximately equal molecular weight (Mr 69,000) by SDS treatment. It is a glycoprotein and can be resolved by disc gel electrophoresis into seven and by isoelectric focusing into more than ten multiple forms. The N-terminal amino acid is serine. | lld:pubmed |
