{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T22:48:41Z","timestamp":1773701321229,"version":"3.50.1"},"reference-count":0,"publisher":"Walter de Gruyter GmbH","issue":"5-6","license":[{"start":{"date-parts":[[1979,6,1]],"date-time":"1979-06-01T00:00:00Z","timestamp":297043200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1979,6,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Two proteins (P\n                    <jats:sub>1<\/jats:sub>\n                    and P\n                    <jats:sub>2<\/jats:sub>\n                    , with mol weights of 57,500 and 27,500, respectively) were isolated from Euglena gracilis. Both proteins show cyanide-insensitive superoxide dismutase activity in the \u201cclassical\u201d superoxide dismutase assay, using xanthine-xanthine oxidase as O\n                    <jats:sub>2<\/jats:sub>\n                    \u00b7\n                    <jats:sup>\u2212<\/jats:sup>\n                    generator. If O\n                    <jats:sub>2<\/jats:sub>\n                    \u00b7\n                    <jats:sup>\u2212<\/jats:sup>\n                    is generated chemically (autoxidation of reduced anthraquinone), photochemically (illuminated riboflavine) or pulse radiolytically, only protein P\n                    <jats:sub>1<\/jats:sub>\n                    but not P\n                    <jats:sub>2<\/jats:sub>\n                    shows SOD activity. Protein P\n                    <jats:sub>1<\/jats:sub>\n                    contains 1 g atom (determined: 0.82) iron (no Mn or Cu) per mole protein and may thus be defined as iron-superoxide dismutase. Protein P\n                    <jats:sub>2<\/jats:sub>\n                    , showing the spectral properties of a flavoprotein, exhibits the activities of ferredoxin-NADP-oxidoreductase and \u201cdiaphorase\u201d. The cyanide-insensitive SOD-activity of this \u201cdiaphorase\u201d in the xanthine oxidase-assay for superoxide dismutase makes this classical and commonly used test unreliable for assaying cyanide insensitive SOD activities. The existence of the \u201cprokaryote-type\u201d of superoxide dismutase (Fe-SOD) in Euglena gracilis is exceptional for an eukaryotic, autotrophically grown organisms.\n                  <\/jats:p>","DOI":"10.1515\/znc-1979-5-609","type":"journal-article","created":{"date-parts":[[2018,8,2]],"date-time":"2018-08-02T13:32:30Z","timestamp":1533216750000},"page":"374-380","source":"Crossref","is-referenced-by-count":15,"title":["Cyanide Insensitive Iron Superoxide Dismutase in Euglena gracilis Comparison of the Reliabilities of Different Test Systems for Superoxide Dismutases"],"prefix":"10.1515","volume":"34","author":[{"given":"E.","family":"Lengfelder","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Strahlenbiologie der Universit\u00e4t M\u00fcnchen, Bavariaring 19, D-8000 M\u00fcnchen 2 E."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E. F.","family":"Elstner","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Botanik und Mikrobiologie, Technische Universit\u00e4t M\u00fcnchen, Arcisstra\u00dfe 21, D-8000 M\u00fcnchen 2"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"374","published-online":{"date-parts":[[2014,6,2]]},"container-title":["Zeitschrift f\u00fcr Naturforschung C"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.degruyter.com\/view\/journals\/znc\/34\/5-6\/article-p374.xml","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/znc-1979-5-609\/xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/znc-1979-5-609\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T21:56:30Z","timestamp":1773698190000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.degruyterbrill.com\/document\/doi\/10.1515\/znc-1979-5-609\/html"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1979,6,1]]},"references-count":0,"journal-issue":{"issue":"5-6","published-online":{"date-parts":[[2014,6,2]]},"published-print":{"date-parts":[[1979,6,1]]}},"alternative-id":["10.1515\/znc-1979-5-609"],"URL":"https:\/\/doi.org\/10.1515\/znc-1979-5-609","relation":{},"ISSN":["1865-7125","0939-5075"],"issn-type":[{"value":"1865-7125","type":"electronic"},{"value":"0939-5075","type":"print"}],"subject":[],"published":{"date-parts":[[1979,6,1]]}}}