scholarly journals Differential phosphorylation of basic and acidic ribosomal proteins by protein kinases bound to membrane-free rat liver polysomes

FEBS Letters ◽  
1979 ◽  
Vol 99 (2) ◽  
pp. 261-264 ◽  
Author(s):  
A. Genot ◽  
J.P. Reboud ◽  
Y. Cenatiempo ◽  
A.J. Cozzone
1994 ◽  
Vol 269 (31) ◽  
pp. 20040-20046 ◽  
Author(s):  
N.A. Morrice ◽  
B. Gabrielli ◽  
B.E. Kemp ◽  
R.E. Wettenhall

Hepatology ◽  
2002 ◽  
Vol 36 (1) ◽  
pp. 72-80 ◽  
Author(s):  
Hajime Nishio ◽  
Hiroko Kuwabara ◽  
Hiroshi Mori ◽  
Koichi Suzuki

FEBS Letters ◽  
1979 ◽  
Vol 104 (1) ◽  
pp. 193-196 ◽  
Author(s):  
I. Toots ◽  
A. Metspalu ◽  
A. Lind ◽  
M. Saarma ◽  
R. Villems

1975 ◽  
Vol 53 (9) ◽  
pp. 935-942 ◽  
Author(s):  
Nabil Hanna ◽  
Claude Godin

Rat liver ribosomes were dissociated into subunits using EDTA, sodium pyrophosphate, high concentrations of KCl, as well as by incubation with puromycin in presence of 0.5 M KCl. The subunits obtained were analyzed using the density gradient centrifugation technique and their ribosomal proteins were separated by means of two-dimensional polyacrylamide gel electrophoresis. The ribosomal protein patterns of the two subunits isolated using each of the dissociating method were compared to the protein patterns of monosomes prepared by puromycin treatment alone. Our results revealed that the use of chelating agents to dissociate the ribosomes resulted in the loss of some ribosomal proteins from the small subunit. On the other hand, the use of KCl in high concentrations to dissociate the ribsosomes did not appear to cause any major loss of proteins from the ribosomes except for some acidic proteins.


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