Synthesis of diphthamide: the target of diphtheria toxin catalyzed ADP-ribosylation in protein synthesis elongation factor 2

1992 ◽  
Vol 114 (4) ◽  
pp. 1495-1496 ◽  
Author(s):  
David A. Evans ◽  
Kristin M. Lundy
2002 ◽  
Vol 69 (2) ◽  
pp. 205-212 ◽  
Author(s):  
CLAUS T. CHRISTOPHERSEN ◽  
JAKOB KARLSEN ◽  
METTE O. NIELSEN ◽  
BENT RIIS

The amount of protein synthesis translational elongation factor 2 (eEF-2) was estimated employing diphtheria toxin-dependent ADP-ribosylation in samples prepared from small amounts of tissue from mammary gland, skeletal muscle and liver from lactating dairy cows. A very high level of ADP-ribosylatable eEF-2 was found in mammary gland, amounting to 20-times the level found in liver and 50-times the level found in skeletal muscle. This obviously reflects the high protein synthesis activity in mammary tissue. To our knowledge, similar high activities have previously been reported only for cancer cells. A close linear relationship was found between the amount of diphtheria-toxin catalysed ADP-ribosylated eEF-2 and protein and casein output in milk from cows in late lactation. This strongly suggests that eEF-2 may be a limiting factor in milk protein synthesis.


FEBS Letters ◽  
1985 ◽  
Vol 191 (2) ◽  
pp. 191-194 ◽  
Author(s):  
A. Giovane ◽  
C. Balestrieri ◽  
L. Quagliuolo ◽  
L. Servillo

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