scholarly journals Purification and characterization of a nuclear protein kinase from rat liver and a hepatoma that is capable of activating poly(A) polymerase.

1984 ◽  
Vol 259 (23) ◽  
pp. 14481-14485
Author(s):  
D A Stetler ◽  
B L Seidel ◽  
S T Jacob
Keyword(s):  
Protein Kinase ◽  
Rat Liver ◽  
Nuclear Protein ◽  
Purification And Characterization

scholarly journals Purification and characterization of the protein kinase eEF-2 isolated from rat liver cells.

1994 ◽  
Vol 41 (4) ◽  
pp. 421-427
Author(s):  
A Gajko ◽  
W Gałasiński ◽  
A Gindzieński
Keyword(s):  
Protein Kinase ◽  
Rat Liver ◽  
Elongation Factor ◽  
Liver Cells ◽  
Relative Molecular Mass ◽  
Purification And Characterization ◽  
Elongation Factor 2 ◽  
Inactive Form ◽  
Rat Liver Cells

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+.

scholarly journals Purification of rat liver nuclear protein kinase NI

1978 ◽  
Vol 253 (13) ◽  
pp. 4638-4641
Author(s):  
W. Thornburg ◽  
A.F. O'Malley ◽  
T.J. Lindell
Keyword(s):  
Protein Kinase ◽  
Rat Liver ◽  
Nuclear Protein
Sign in / Sign up

Export Citation Format

Share Document