| dc.contributor.author | Nurten, Rüstem | |
| dc.contributor.author | Gökçe, Sina | |
| dc.contributor.author | Bektas, Muhammet | |
| dc.contributor.author | Ergen, Kivanc | |
| dc.date.accessioned | 2021-03-02T21:49:12Z | |
| dc.date.available | 2021-03-02T21:49:12Z | |
| dc.date.issued | 2007 | |
| dc.identifier.citation | Ergen 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.issn | 0327-9545 | |
| dc.identifier.other | vv_1032021 | |
| dc.identifier.other | av_090fd038-39ce-49a6-b7fd-118a1c65d852 | |
| dc.identifier.uri | http://hdl.handle.net/20.500.12627/11895 | |
| dc.description.abstract | Eukaryotic 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.iso | eng | |
| dc.subject | Tıbbi Biyoloji | |
| dc.subject | Yaşam Bilimleri | |
| dc.subject | Temel Bilimler | |
| dc.subject | Temel Tıp Bilimleri | |
| dc.subject | Biyokimya | |
| dc.subject | Sağlık Bilimleri | |
| dc.subject | Tıp | |
| dc.subject | Yaşam Bilimleri (LIFE) | |
| dc.subject | Biyoloji ve Biyokimya | |
| dc.subject | BİYOLOJİ | |
| dc.title | Endogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment | |
| dc.type | Makale | |
| dc.relation.journal | BIOCELL | |
| dc.contributor.department | , , | |
| dc.identifier.volume | 31 | |
| dc.identifier.issue | 1 | |
| dc.identifier.startpage | 61 | |
| dc.identifier.endpage | 66 | |
| dc.contributor.firstauthorID | 6925 | |
