{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,15]],"date-time":"2025-10-15T17:37:00Z","timestamp":1760549820809},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1973,7,1]]},"abstract":"<jats:p>1. Acetylcholinesterase from human erythrocytes was solubilized with Triton X-100 in strong salt solution and partially purified by (NH4)2SO4 fractionation. This preparation showed three main bands of enzyme activity after electrophoresis on polyacrylamide gel and incubation with either \u03b1-naphthyl acetate or acetylthiocholine as enzyme substrate. Two of the multiple forms were completely inhibited by 10\u03bcm-eserine and one only partially. Treatment with neuraminidase had no effect on the electrophoretic pattern; therefore sialic acid does not appear to determine or affect the ratios of the acetylcholinesterase multiple forms, unlike those of the serum cholinesterase. 2. Chromatography of the preparation on Sephadex G-200 revealed one major peak of enzyme activity and a suggestion of two minor zones of mol.wt. 546000, 184000 and 93000 (i.e. in the proportion 6:2:1). The main peak was almost completely separated from the Triton X-100 and the overall purification was about 600-fold. Further attempts to purify the enzyme by absorption on calcium phosphate gels were unsuccessful. 3. Electrophoresis of the enzyme preparation on a polyacrylamide gradient for 24h revealed three main bands that corresponded to the three values for molecular weights obtained by column chromatography. After 70h of electrophoresis a further three zones of activity developed making six molecular entities, the molecular weights of which were simple multiples of a monomer, thus resembling the cholinesterase found in serum.<\/jats:p>","DOI":"10.1042\/bj1330521","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T19:49:22Z","timestamp":1439236162000},"page":"521-527","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":46,"title":["Multiple forms of acetylcholinesterase from human erythrocytes"],"prefix":"10.1042","volume":"133","author":[{"given":"David L.","family":"Wright","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Chelsea College, London SW3 6LX, U.K."}]},{"given":"David T.","family":"Plummer","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Chelsea College, London SW3 6LX, U.K."}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/133\/3\/521\/561009\/bj1330521.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/133\/3\/521\/561009\/bj1330521.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T15:08:18Z","timestamp":1637939298000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/133\/3\/521\/7813\/Multiple-forms-of-acetylcholinesterase-from-human"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1973,7,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1973,7,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1330521","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1973,7,1]]}}}