{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T01:57:30Z","timestamp":1760061450048},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1976,6,1]]},"abstract":"<jats:p>Alkaline phosphatase from human liver was purified to homogeneity. The purification procedure included solubilization with butanol, fractionation with acetone, and chromatography on concanavalin A-Sepharose, DEAE-cellulose, Sephadex G-200 and DEAE-Sephadex. Purity was established by standard and sodium dodecyl sulphate\/polyacrylamide-gel electrophoresis. The isoelectric point of the protein was determined to be 4.0. Sephadex-gel filtration gave a mol.wt. of 146000, although a higher value was obtained in the presence of 100mM-NaC1. The subunit mol.wt. 76700, was determined by sodium dodecyl sulphate\/polyacrylamide-gel electrophoresis. Neuraminidase treatment resulted in two enzyme-activity bands on isoelectric-focused gels with isoelectric points of 6.6 and 6.8. The desialylated enzyme gave only one protein band on sodium dodecyl sulphate\/polyacrylamide-gel electrophoresis with a subunit molecular weight indistinguishable from that of the non-neuraminidase-treated protein. The desialylated enzyme was more readily denatured by sodium dodecyl sulphate in the presence of mercaptoethanol than was the native enzyme.<\/jats:p>","DOI":"10.1042\/bj1550653","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:02:55Z","timestamp":1439236975000},"page":"653-660","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":69,"title":["Affinity purification and some molecular properties of human liver alkaline phosphatase"],"prefix":"10.1042","volume":"155","author":[{"given":"J M","family":"Tr\u00e9panier","sequence":"first","affiliation":[{"name":"Department of Pathology, Division of Medical Laboratory Science, University of Alberta, Edmonton, Alberta T6G 2G3, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L E","family":"Seargeant","sequence":"additional","affiliation":[{"name":"Department of Pathology, Division of Medical Laboratory Science, University of Alberta, Edmonton, Alberta T6G 2G3, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R A","family":"Stinson","sequence":"additional","affiliation":[{"name":"Department of Pathology, Division of Medical Laboratory Science, University of Alberta, Edmonton, Alberta T6G 2G3, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/155\/3\/653\/616386\/bj1550653.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/155\/3\/653\/616386\/bj1550653.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T17:18:16Z","timestamp":1637947096000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/155\/3\/653\/10861\/Affinity-purification-and-some-molecular"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1976,6,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1976,6,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1550653","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1976,6,1]]}}}