{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T10:43:08Z","timestamp":1758278588577},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1979,9,1]]},"abstract":"<jats:p>Goblet-cell mucin (mucin 1) was isolated and purified from human small-intestinal scrapings. After application of mucin 1 to DEAE-Bio-Gel (A) columns, most of the glycoprotein (76\u201394% of hexoses) was eluted in the first peak (designated mucin 2). Minor amounts of acidic glycoproteins were eluted with 0.2m- and 0.4m-NaCl in later peaks. Analyses of mucin 1 and mucin 2 revealed mucin 2 to be a monodisperse highly glycosylated glycoprotein containing 6.3% by wt. of protein, N-acetylgalactosamine, N-acetylglucosamine, galactose and fucose. Mucin 1 was similar in composition, but was polydisperse and contained more protein (12.3% by wt.) as well as N-acetylneuraminic acid. Analytical CsCl-gradient ultracentrifugation showed both mucin 1 and mucin 2 to have a major component with an average buoyant density of 1.47000g\/ml. Mucin 1 also contained a slightly less-dense minor glycoprotein component. After exhaustive reduction and alkylation mucin 1 retained its major component, but partly dissociated into two lighter glycoprotein components. Mucin 2, in contrast, did not change its density distribution after reduction. Band ultracentrifugation in 2H2O-containing iso-osmotic buffers showed that mucin 1 contained a major fast-sedimenting component (so=37\u00b12S), and a minor amount of a slower-sedimenting component. After reduction there was an increased quantity of the latter component, for which an so value of 14.5S was calculated. In contrast, mucin 2 was unaltered by reduction (so=33\u00b12S). These findings indicate that the major component of goblet-cell mucin (mucin 2) does not dissociate after S\u2013S-bond reduction, and thus does not apparently rely for its polymeric structure on the association of subunits through covalent disulphide bonds. However, the effects of reduction on mucin 1 suggest that in the native mucin intramolecular disulphide bonds in the minor glycoproteins may stabilize their structure, permitting secondary non-covalent interactions to develop with the major dense mucin (mucin 2) protein.<\/jats:p>","DOI":"10.1042\/bj1810725","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:16:50Z","timestamp":1439237810000},"page":"725-732","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["The role of disulphide bonds in human intestinal mucin"],"prefix":"10.1042","volume":"181","author":[{"given":"Janet F.","family":"Forstner","sequence":"first","affiliation":[{"name":"Research Institute, The Hospital for Sick Children, Toronto, Ont., Canada M5G 1X8"},{"name":"Department of Biochemistry, University of Toronto, Toronto, Ont., Canada M5S 1A8"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Inderjit","family":"Jabbal","sequence":"additional","affiliation":[{"name":"Research Institute, The Hospital for Sick Children, Toronto, Ont., Canada M5G 1X8"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rauf","family":"Qureshi","sequence":"additional","affiliation":[{"name":"Research Institute, The Hospital for Sick Children, Toronto, Ont., Canada M5G 1X8"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David I. C.","family":"Kells","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Toronto, Toronto, Ont., Canada M5S 1A8"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gordon G.","family":"Forstner","sequence":"additional","affiliation":[{"name":"Research Institute, The Hospital for Sick Children, Toronto, Ont., Canada M5G 1X8"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/181\/3\/725\/572471\/bj1810725.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/181\/3\/725\/572471\/bj1810725.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T13:08:37Z","timestamp":1637932117000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/181\/3\/725\/4345\/The-role-of-disulphide-bonds-in-human-intestinal"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1979,9,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1979,9,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1810725","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1979,9,1]]}}}