{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T15:04:34Z","timestamp":1781103874946,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"4","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1975,4]]},"abstract":"<jats:p>Rat liver mitochondria contain a Mg2+-requiring system that transfers the ADP-ribose moiety of NAD+ to an acceptor protein. The enzyme system was extracted in a soluble form and the ADP-ribosylated protein product was isolated by hydroxyapatite and Sephadex chromatography. The ADP-ribosylated protein product has a molecular weight of 100,000 and can be dissociated into subunits of 50,000 daltons by sodium dodecyl sulfate gel electrophoresis. Incubation of the isotopically labeled ADP-ribosylated protein with nicotinamide and a mitochondrial extract yields labeled NAD+, indicating apparent reversibility of the reaction. Enzymatic degradation of the ADP-ribosylated protein with snake venom phosphodiesterase liberates AMP and ADP-ribose or its isomer. Identification of these products and reversibility of the reaction show that the ADP-ribose moiety of NAD+ is the molecular species that is transferred to the acceptor protein. A fraction of the protein-bound ADP-ribose appears to be present as an an oligomer. The enzymatic protein-ADP-ribosylating reaction is inhibited by nicotinamide, ADP-ribose, the fluorophosphate of AMP, and picrylsulfonic acid.<\/jats:p>","DOI":"10.1073\/pnas.72.4.1436","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T03:05:56Z","timestamp":1149044756000},"page":"1436-1440","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":68,"title":["Macromolecular enzymatic product of NAD+ in liver mitochondria."],"prefix":"10.1073","volume":"72","author":[{"given":"E","family":"Kun","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P H","family":"Zimber","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A C","family":"Chang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B","family":"Puschendorf","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"H","family":"Grunicke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1975,4]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.72.4.1436","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T11:03:27Z","timestamp":1649847807000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.72.4.1436"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1975,4]]},"references-count":0,"journal-issue":{"issue":"4","published-print":{"date-parts":[[1975,4]]}},"alternative-id":["10.1073\/pnas.72.4.1436"],"URL":"https:\/\/doi.org\/10.1073\/pnas.72.4.1436","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1975,4]]},"assertion":[{"value":"1975-04-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}