{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,8]],"date-time":"2025-10-08T22:14:37Z","timestamp":1759961677194},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1975,7,1]]},"abstract":"<jats:p>Assay methods were developed enabling separate determination of N- and O-sulphotransferase activities in an enzyme preparation from mouse mastocytoma. N-Desulphoheparin and chemically N-acetylated heparan sulphate were used as specific exogenous sulphate acceptors in the transfer of [35S]sulphate residues from adenosine 3'-phosphate 5'-[35S]sulphatophosphate to amino and hydroxyl groups respectively. The resulting 35S-labelled polysaccharides were isolated as their cetylpyridinium complexes on filter paper. Sulphotransferases were solubilized from a mastocytoma microsomal fraction by treatment with detergent-alkali. The pH optimum for both enzymes was about 7.5 Km with regard to adenosine 3'-phosphate 5'-sulphatophosphate was estimated to be 2 \u00d7 10-5 M for the N-sulphotransferase and 1 \u00d7 10-4 M for the O-sulphotransferase(s). The enzymes required bivalent cations for maximum activity, Mn2+ stimulating both the N- and O-sulphotransferase four- to five-fold, whereas Ca2+ increased the N- but not the O-sulphotransferase activity. The O-sulphotransferase was found to be more sensitive to heat-inactivation, 60% of the activity being lost after 1 min at 50 degrees C, whereas only 15% of the N-sulphotransferase activity was lost. In contrast, the N-sulphotransferase was selectively inhibited (or inactivated) by NaCl; at 0.125 M-NaCl concentration the O-sulphotransferase activity was essentially unaffected, whereas the N-sulphotransferase activity was depressed by 80%. These results strongly indicate that N- and O-sulphate-transfer reactions should be ascribed to different enzymes, or, alternatively, to separate and independent active sites on the same enzyme molecule.<\/jats:p>","DOI":"10.1042\/bj1490049","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T19:58:38Z","timestamp":1439236718000},"page":"49-55","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":40,"title":["Biosynthesis of heparin. Solubilization and partial characterization of <i>N<\/i>- and <i>O<\/i>-sulphotransferases"],"prefix":"10.1042","volume":"149","author":[{"given":"L","family":"Jansson","sequence":"first","affiliation":[{"name":"Institute of Medical and Physiological Chemistry, University of Uppsala, Sweden, and"}]},{"given":"M","family":"H\u00f6\u00f6k","sequence":"additional","affiliation":[{"name":"Institute of Medical and Physiological Chemistry, University of Uppsala, Sweden, and"}]},{"given":"\u00c5","family":"Wasteson","sequence":"additional","affiliation":[{"name":"Institute of Medical and Physiological Chemistry, University of Uppsala, Sweden, and"}]},{"given":"U","family":"Lindahl","sequence":"additional","affiliation":[{"name":"Department of Medical Chemistry, Swedish Veterinary College, Biomedical Center, S-751 23 Uppsala, Sweden"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/149\/1\/49\/565190\/bj1490049.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/149\/1\/49\/565190\/bj1490049.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T16:55:24Z","timestamp":1637945724000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/149\/1\/49\/10042\/Biosynthesis-of-heparin-Solubilization-and-partial"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1975,7,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1975,7,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1490049","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1975,7,1]]}}}