{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,8]],"date-time":"2026-01-08T15:59:43Z","timestamp":1767887983681,"version":"3.49.0"},"reference-count":39,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2004,9,22]],"date-time":"2004-09-22T00:00:00Z","timestamp":1095811200000},"content-version":"vor","delay-in-days":2397,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Journal of Physiology"],"published-print":{"date-parts":[[1998,3]]},"abstract":"<jats:p>\n<jats:list list-type=\"explicit-label\">\n<jats:list-item><jats:p>Luminal membrane vesicles (LMV) were isolated from human and pig colonic tissues. They were characterized in terms of purity and ability to transport [<jats:sup>14<\/jats:sup>C]butyrate.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The activity of cysteine\u2010sensitive alkaline phosphatase, and the abundance of villin, NHE2 and NHE3 proteins, markers of the colonic luminal membrane, were significantly enriched in the LMV compared with the original cellular homogenate. The LMV were free from contamination by other cellular organelles and basolateral membranes, as revealed by the negligible presence of either specific marker enzyme activity or characteristic immunogenic protein.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The transport of butyrate into the luminal membrane vesicles was enhanced 5\u2010fold at pH 5.5 compared with pH 8.0. Butyrate transport was temperature dependent, and was stimulated in the presence of an outward\u2010directed anion gradient in the order of butyrate &gt; bicarbonate &gt; propionate &gt; chloride. Kinetic analysis of increasing substrate concentration showed saturation kinetics with an apparent <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> value of 14.8 \u00b1 3.6 mM and a <jats:italic>V<\/jats:italic><jats:sub>max<\/jats:sub> of 54 \u00b1 14 nmol min<jats:sup>\u22121<\/jats:sup> (mg protein)<jats:sup>\u22121<\/jats:sup>.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>Butyrate transport was significantly reduced in the presence of short chain fatty acids (SCFA), acetate, propionate and other monocarboxylates (pyruvate and L\u2010lactate). Butyrate uptake was inhibited by several cysteine group modifying reagents such as <jats:italic>p<\/jats:italic>\u2010chloromercuribenzosulphonic acid (pCMBS), <jats:italic>p<\/jats:italic>\u2010chloromercuribenzoate (pCMB), mersalyl acid and HgCl<jats:sub>2<\/jats:sub>, but not by the stilbene anion exchange inhibitors, 4,4\u2032\u2010diisothiocyanostilbene\u20102,2\u2032\u2010disulphonate (DIDS) and 4,4\u2032\u2010dinitrostilbene\u20102,2\u2032\u2010disulphonate (SITS).<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The described properties of butyrate transport across the luminal pole of the colon suggest the involvement of a carrier protein, in the form of a pH\u2010activated anion exchange process. The transporter is distinct from the erythrocyte band\u20103 type anion exchanger and may belong to the monocarboxylate\u2010type transport proteins (MCT1).<\/jats:p><\/jats:list-item>\n<\/jats:list>\n<\/jats:p>","DOI":"10.1111\/j.1469-7793.1998.819bs.x","type":"journal-article","created":{"date-parts":[[2004,9,22]],"date-time":"2004-09-22T09:53:43Z","timestamp":1095846823000},"page":"819-830","source":"Crossref","is-referenced-by-count":100,"title":["The characterization of butyrate transport across pig and human colonic luminal membrane"],"prefix":"10.1113","volume":"507","author":[{"given":"Armin","family":"Ritzhaupt","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Antony","family":"Ellis","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ken B.","family":"Hosie","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Soraya P.","family":"Shirazi\u2010Beechey","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2004,9,22]]},"reference":[{"key":"e_1_2_5_1_1","doi-asserted-by":"publisher","DOI":"10.1152\/physrev.1990.70.2.567"},{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1093\/carcin\/9.3.447"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2736(84)90093-2"},{"key":"e_1_2_5_4_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.76.5.2321"},{"key":"e_1_2_5_5_1","doi-asserted-by":"publisher","DOI":"10.1136\/gut.32.8.923"},{"key":"e_1_2_5_6_1","first-page":"89","article-title":"Colonic absorption: The importance of SCFA in man","volume":"19","author":"Cummings J. 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