{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T16:44:40Z","timestamp":1781109880348,"version":"3.54.1"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"2","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1989,1]]},"abstract":"<jats:p>Polyoma virus-transformed baby hamster kidney (pyBHK) cells were cultured in medium containing [32P]orthophosphate and 10% (vol\/vol) fetal bovine serum. A 32P-labeled protein with an apparent molecular mass of 97 kDa was immunoprecipitated from cell lysates with antiserum to ADP-ribosylated elongation factor 2 (EF-2). The 32P labeling of the protein was enhanced by culturing cells in medium containing 2% serum instead of 10% serum. The 32P label was completely removed from the protein by treatment with snake venom phosphodiesterase and the digestion product was identified as [32P]AMP, indicating the protein was mono-ADP-ribosylated. HPLC analysis of tryptic peptides of the 32P-labeled 97-kDa protein and purified EF-2, which was ADP-ribosylated in vitro with diphtheria toxin fragment A and [32P]NAD, demonstrated an identical labeled peptide in the two proteins. The data strongly suggest that EF-2 was endogenously ADP-ribosylated in pyBHK cells. Maximum incorporation of radioactivity in EF-2 occurred by 12 hr and remained constant over the subsequent 12 hr. It was estimated that 30-35% of the EF-2 was ADP-ribosylated in cells cultured in medium containing 2% serum. When 32P-labeled cultures were incubated in medium containing unlabeled phosphate, the 32P label was lost from the EF-2 within 30 min.<\/jats:p>","DOI":"10.1073\/pnas.86.2.554","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T07:05:40Z","timestamp":1149059140000},"page":"554-557","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":44,"title":["Endogenous ADP-ribosylation of elongation factor 2 in polyoma virus-transformed baby hamster kidney cells."],"prefix":"10.1073","volume":"86","author":[{"given":"J L","family":"Fendrick","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, University of Rochester, NY 14642."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"W J","family":"Iglewski","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of Rochester, NY 14642."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1989,1]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.86.2.554","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T12:44:35Z","timestamp":1649853875000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.86.2.554"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1989,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1989,1]]}},"alternative-id":["10.1073\/pnas.86.2.554"],"URL":"https:\/\/doi.org\/10.1073\/pnas.86.2.554","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1989,1]]},"assertion":[{"value":"1989-01-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}