Introduction of Additional Charges as an Aid in Protein Purification: Isolation of Elongation Factor 2 from Sulfolobus acidocaldarius by Preparative Isoelectric Focusing Before and After ADP-Ribosylation

1994 ◽  
Vol 5 (6) ◽  
pp. 553-558
Author(s):  
K.D. Siegmund ◽  
F. Klink
Keyword(s):  
Protein Purification ◽  
Isoelectric Focusing ◽  
Elongation Factor ◽  
Sulfolobus Acidocaldarius ◽  
Adp Ribosylation ◽  
Elongation Factor 2 ◽  
Before And After ◽  
Additional Charges

Endogenous ADP-ribosylation of elongation factor-2 by interleukin-1β

2010 ◽  
Vol 348 (1-2) ◽  
pp. 125-128 ◽  
Author(s):  
Doris Jäger ◽  
Karl Werdan ◽  
Ursula Müller-Werdan
Keyword(s):  
Elongation Factor ◽  
Interleukin 1Β ◽  
Adp Ribosylation ◽  
Elongation Factor 2

Distribution of elongation factor 2 between particulate and soluble fractions of the brine shrimp Artemia during early development

1983 ◽  
Vol 61 (8) ◽  
pp. 833-839 ◽  
Author(s):  
Z. Yablonka-Reuveni ◽  
J. J. Fontaine ◽  
A. H. Warner
Keyword(s):  
Early Development ◽  
Subcellular Distribution ◽  
Brine Shrimp ◽  
Elongation Factor ◽  
Stages Of Development ◽  
Adp Ribosylation ◽  
Elongation Factor 2 ◽  
Soluble Fractions

The ADP-ribosylation of elongation factor 2 (EF-2) in vitro was used to quantitate EF-2 and to determine its subcellular distribution in extracts of Artemia embryos at different stages of development. In extracts from dormant cysts of Artemia 40–45% of EF-2 is complexed to macromolecules smaller than ribosomes, whereas the remainder is soluble or free in the cytosol. During early development the amount of "complexed" EF-2 decreases markedly concomitant with an increase in the pool of soluble EF-2. Complexed EF-2 was found to be associated with macromolecules which sediment at 16S–20S and 40S–50S and not with monoribosomes or polyribosomes as reported for mammalian systems. The data show that the decrease in complexed EF-2 is associated with the resumption of development in Artemia.

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