@Article{biocell.2007.31.061,
AUTHOR = {KIVANÇ ERGEN, MUHAMMET BEKTAŞ, SINA GÖKÇE,  RÜSTEM NURTEN},
TITLE = {Endogenous ADP-ribosylation of eukaryotic elongation factor 2 and its 32 kDa tryptic fragment},
JOURNAL = {BIOCELL},
VOLUME = {31},
YEAR = {2007},
NUMBER = {1},
PAGES = {61--66},
URL = {http://www.techscience.com/biocell/v31n1/33904},
ISSN = {1667-5746},
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.<br/>
In our study, the elution of 32F from SDS-PAGE was ADP-ribosylated both in the presence and absence of
diphtheria toxin. These results suggest that endogenous ADP-ribosylation of 32F might be related to protein
synthesis. This modification appears to be important for the cell function.},
DOI = {10.32604/biocell.2007.31.061}
}