Partial purification of a tyrosyl protein kinase from rat liver cytosol by affinity chromatography on poly(Glu:Tyr)-linked Sepharose 4B

1988 ◽  
Vol 16 (5) ◽  
pp. 780-780
Author(s):  
DAVID MANGNALL ◽  
JOHN BERESFORD ◽  
ANDREW PRESCOTT
Keyword(s):  
Protein Kinase ◽  
Affinity Chromatography ◽  
Rat Liver ◽  
Partial Purification ◽  
Liver Cytosol ◽  
Sepharose 4B ◽  
Rat Liver Cytosol

Partial purification of a cortisol binding protein from rat liver cytosol

Steroids ◽  
1970 ◽  
Vol 16 ◽  
pp. 207-216 ◽  
Author(s):  
M. Beato ◽  
W. Schmid ◽  
W. Braendle ◽  
C.E. Sekeris
Keyword(s):  
Rat Liver ◽  
Binding Protein ◽  
Partial Purification ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Effect of starvation, diabetes and insulin on the casein kinase 2 from rat liver cytosol

1985 ◽  
Vol 225 (2) ◽  
pp. 321-326 ◽  
Author(s):  
C Martos ◽  
M Plana ◽  
M D Guasch ◽  
E Itarte
Keyword(s):  
Rat Liver ◽  
Glycogen Synthase ◽  
Gradient Centrifugation ◽  
Diabetic Rats ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Partial Purification ◽  
Liver Cytosol ◽  
Casein Kinases ◽  
Rat Liver Cytosol

Starvation, diabetes and insulin did not alter the concentration of casein kinases in rat liver cytosol. However, the Km for casein of casein kinase 2 from diabetic rats was about 2-fold lower than that from control animals. Administration of insulin to control rats did not alter this parameter, but increased the Km for casein of casein kinase 2 in diabetic rats. Starvation did not affect the kinetic constants of casein kinases. The effect of diabetes on casein kinase 2 persisted after partial purification of the enzyme by glycerol-density-gradient centrifugation and affected also its activity on other protein substrates such as phosvitin, high-mobility-group protein 14 and glycogen synthase. The results indicate that rat liver cytosol casein kinase 2 is under physiological control.

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