{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,9,15]],"date-time":"2024-09-15T19:27:12Z","timestamp":1726428432525},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1987,2,15]]},"abstract":"<jats:p>Chicken caecal arylsulphatase was purified 700-fold by (NH4)2SO4 fractionation, concanavalin A-Sepharose and cyclic AMP-Sepharose chromatographies. The purified enzyme was a glycoprotein of Mr 97,000. It hydrolysed p-nitrocatechol sulphate, cerebroside 3-sulphate and ascorbic acid 2-sulphate and was strongly inhibited by Na2SO4 (Ki = 50 microM) and Na3PO4 (Ki = 20 microM). Arylsulphatase from Eimeria tenella sporozoites was purified 28-fold by (NH4)2SO4 fractionation. Arylsulphatase of E. tenella sporozoites was not a glycoprotein. It had an Mr of 49,000. It was inhibited by Na2SO4 (Ki = 300 microM), sodium phosphate (Ki = 90 microM) and heparin. It hydrolysed ascorbic acid 2-sulphate, but cerebroside 3-sulphate was not desulphated. The kinetic parameters of chicken caecal arylsulphatase were different from those of the E. tenella enzyme.<\/jats:p>","DOI":"10.1042\/bj2420097","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T16:57:48Z","timestamp":1439225868000},"page":"97-102","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Comparison of arylsulphatases from <i>Eimeria tenella<\/i> (parasite) and chicken caecum (host)"],"prefix":"10.1042","volume":"242","author":[{"given":"A A","family":"Farooqui","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"W L","family":"Hanson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/242\/1\/97\/590375\/bj2420097.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/242\/1\/97\/590375\/bj2420097.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T12:03:13Z","timestamp":1637841793000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/242\/1\/97\/22826\/Comparison-of-arylsulphatases-from-Eimeria-tenella"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1987,2,15]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1987,2,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2420097","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"type":"print","value":"0264-6021"},{"type":"electronic","value":"1470-8728"}],"subject":[],"published":{"date-parts":[[1987,2,15]]}}}