{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,2]],"date-time":"2026-01-02T17:25:10Z","timestamp":1767374710962},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1977,9,1]]},"abstract":"<jats:p>Microsomal UDP-glucuronyltransferase and cytosolic sulphotransferase share many substrates, such as phenols and hydroxamic acids. In a search for a selective inhibitor of sulphation, several phenolic compounds were tested. 2,6-Dichloro-4-nitrophenol is introduced as a selective inhibitor of sulphation in vivo, having no effect on UDP-glucuronyltransferase activity. As substrate for both conjugating enzymes the phenolic drug harmol (7-hydroxy-1-methyl-9H-pyrido[3,4-b]indole) was used. In the rat in vivo 2,6-dichloro-4-nitrophenol caused almost complete inhibition of harmol sulphation after a single intraperitoneal injection (26\u03bcmol\/kg) for 48h; the percentage of harmol sulphated decreased from 75% in controls to 5% in the treated rats. The percentage of harmol glucuronidated increased from 25 to 95%. Pentachlorophenol was equally effective but also highly toxic. Salicylamide had only a very-short-lasting inhibitory effect on sulphation. In vitro, 2,6-dichloro-4-nitrophenol inhibited sulphation of harmol by a rat liver postmitochondrial supernatant completely at 1\u03bcm, whereas even at 100\u03bcm it had no effect on glucuronidation of harmol. It is concluded that 2,6-dichloro-4-nitrophenol is a selective inhibitor of sulphation and, further, that its long duration of action makes it suitable for studies on the regulatory role of sulphation in some biological processes.<\/jats:p>","DOI":"10.1042\/bj1650553","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:07:35Z","timestamp":1439237255000},"page":"553-559","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":111,"title":["Phenol sulphotransferase and uridine diphosphate glucuronyltransferase from rat liver <i>in vivo<\/i> and <i>in vitro<\/i>. 2,6-Dichloro-4-nitrophenol as selective inhibitor of sulphation"],"prefix":"10.1042","volume":"165","author":[{"given":"Gerard J.","family":"Mulder","sequence":"first","affiliation":[{"name":"Department of Pharmacology, State University of Groningen, Groningen, The Netherlands"}]},{"given":"Egbert","family":"Scholtens","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, State University of Groningen, Groningen, The Netherlands"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/165\/3\/553\/568741\/bj1650553.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/165\/3\/553\/568741\/bj1650553.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T17:40:37Z","timestamp":1637948437000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/165\/3\/553\/11382\/Phenol-sulphotransferase-and-uridine-diphosphate"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1977,9,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1977,9,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1650553","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1977,9,1]]}}}