{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T10:56:43Z","timestamp":1758279403952},"reference-count":0,"publisher":"Canadian Science Publishing","issue":"6","license":[{"start":{"date-parts":[[1979,6,1]],"date-time":"1979-06-01T00:00:00Z","timestamp":297043200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.nrcresearchpress.com\/page\/about\/CorporateTextAndDataMining"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Can. J. Biochem."],"published-print":{"date-parts":[[1979,6,1]]},"abstract":"<jats:p> Fumarate reductase has been purified 100-fold to 95% homogeneity from the cytoplasmic membrane of Escherichia coli, grown anaerobically on a defined medium containing glycerol plus fumarate. Optimal solubilization of total membrane protein and fumarate reductase activity occurred with nonionic detergents having a hydrophobic\u2013lipophilic balance (HLB) number near 13 and we routinely solubilized the enzyme with Triton X-100 (HLB number\u2002=\u200213.5). Membrane enzyme extracts were fractionated by hydrophobic-exchange chromatography on phenyl Sepharose CL-4B to yield purified enzyme. The enzyme, whether membrane bound, in Triton extracts, or purified, had an apparent K<jats:sub>m<\/jats:sub> near 0.42\u2002mM. Two peptides with molecular weights of 70\u2002000 and 24\u2002000, present in 1:1 molar ratios, were identified by sodium dodecyl sulfate polyacrylamide slab-gel electrophoresis to coincide with enzyme activity. A minimal native molecular weight of 100\u2002000 was calculated for fumarate reductase by Sephacryl S-200 gel filtration in the presence of sodium cholate. This would indicate that the enzyme is a dimer. The purified enzyme has low, but measurable, succinate dehydrogenase activity. <\/jats:p>","DOI":"10.1139\/o79-101","type":"journal-article","created":{"date-parts":[[2009,12,21]],"date-time":"2009-12-21T10:22:18Z","timestamp":1261390938000},"page":"813-821","source":"Crossref","is-referenced-by-count":71,"title":["Purification and characterization of membrane-bound fumarate reductase from anaerobically grown <i>Escherichia coli<\/i>"],"prefix":"10.1139","volume":"57","author":[{"given":"Peter","family":"Dickie","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joel H.","family":"Weiner","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"155","container-title":["Canadian Journal of Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nrcresearchpress.com\/doi\/pdf\/10.1139\/o79-101","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,1,5]],"date-time":"2020-01-05T17:53:00Z","timestamp":1578246780000},"score":1,"resource":{"primary":{"URL":"http:\/\/www.nrcresearchpress.com\/doi\/10.1139\/o79-101"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1979,6,1]]},"references-count":0,"journal-issue":{"issue":"6","published-print":{"date-parts":[[1979,6,1]]}},"alternative-id":["10.1139\/o79-101"],"URL":"https:\/\/doi.org\/10.1139\/o79-101","relation":{},"ISSN":["0008-4018"],"issn-type":[{"value":"0008-4018","type":"print"}],"subject":[],"published":{"date-parts":[[1979,6,1]]}}}