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Endogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment

dc.contributor.authorNurten, Rüstem
dc.contributor.authorGökçe, Sina
dc.contributor.authorBektas, Muhammet
dc.contributor.authorErgen, Kivanc
dc.date.accessioned2021-03-02T21:49:12Z
dc.date.available2021-03-02T21:49:12Z
dc.date.issued2007
dc.identifier.citationErgen K., Bektas M., Gökçe S., Nurten R., "Endogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment", BIOCELL, cilt.31, sa.1, ss.61-66, 2007
dc.identifier.issn0327-9545
dc.identifier.othervv_1032021
dc.identifier.otherav_090fd038-39ce-49a6-b7fd-118a1c65d852
dc.identifier.urihttp://hdl.handle.net/20.500.12627/11895
dc.description.abstractEukaryotic elongation factor 2 (eEF-2) can undergo ADP-ribosylation in the absence of diphtheria toxin. The binding of free ADP-ribose and endogenous transferase-dependent ADP-ribosylation were distinct reactions for eEF-2, as indicated by different findings. Incubation of eEF-2 tryptic fragment 32/33 kDa (32F) with NAD was ADP-ribosylated and gave rise to the covalent binding of ADP-ribose to eEF-2. 32F was revealed to be at the C-terminal by Edman degradation sequence analysis.
dc.language.isoeng
dc.subjectTıbbi Biyoloji
dc.subjectYaşam Bilimleri
dc.subjectTemel Bilimler
dc.subjectTemel Tıp Bilimleri
dc.subjectBiyokimya
dc.subjectSağlık Bilimleri
dc.subjectTıp
dc.subjectYaşam Bilimleri (LIFE)
dc.subjectBiyoloji ve Biyokimya
dc.subjectBİYOLOJİ
dc.titleEndogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment
dc.typeMakale
dc.relation.journalBIOCELL
dc.contributor.department, ,
dc.identifier.volume31
dc.identifier.issue1
dc.identifier.startpage61
dc.identifier.endpage66
dc.contributor.firstauthorID6925


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