KIVANÇ ERGEN*, MUHAMMET BEKTAŞ**, SINA GÖKÇE**, RÜSTEM NURTEN**
BIOCELL, Vol.31, No.1, pp. 61-66, 2007, DOI:10.32604/biocell.2007.31.061
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.
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… More >
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