scholarly journals Purification and characterization of native human elongation factor 2

2019 ◽  
Vol 158 ◽  
pp. 15-19
Author(s):  
Rasmus Kock Flygaard ◽  
Beatrice Malacrida ◽  
Patrick Kiely ◽  
Lasse Bohl Jenner
2011 ◽  
Vol 79 (2) ◽  
pp. 237-244 ◽  
Author(s):  
Olga Abramczyk ◽  
Clint D.J. Tavares ◽  
Ashwini K. Devkota ◽  
Alexey G. Ryazanov ◽  
Benjamin E. Turk ◽  
...  

1994 ◽  
Vol 41 (4) ◽  
pp. 421-427
Author(s):  
A Gajko ◽  
W Gałasiński ◽  
A Gindzieński

The elongation factor 2 (eEF-2) protein kinase was isolated from rat liver cells, purified and partly characterized. It was found that the enzyme exists in an inactive form in the homogenate of rat liver. The active fraction of kinase eEF-2 was obtained after removal of the inhibitory substance by hydroxyapatite column chromatography. The purified enzyme is an electrophoretically homogeneous protein with relative molecular mass of approximately 90,000 and isoelectric point, pI = 5.9. The enzyme specifically phosphorylates the elongation factor eEF-2 in the presence of calmodulin and Ca2+.


1992 ◽  
Vol 267 (2) ◽  
pp. 1190-1197 ◽  
Author(s):  
J P Perentesis ◽  
L D Phan ◽  
W B Gleason ◽  
D C LaPorte ◽  
D M Livingston ◽  
...  

1984 ◽  
Vol 81 (10) ◽  
pp. 3158-3162 ◽  
Author(s):  
Y. Kaneda ◽  
M. C. Yoshida ◽  
K. Kohno ◽  
T. Uchida ◽  
Y. Okada

1992 ◽  
Vol 373 (1) ◽  
pp. 201-204 ◽  
Author(s):  
Jozef HANES ◽  
Johannes FREUDENSTEIN ◽  
Georg RAPP ◽  
Karl Heinz SCHEIT

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