Structural and functional properties of protein synthesis initiation factors eIF-2 and eIF-2B from rat liver

1985 ◽  
Vol 13 (4) ◽  
pp. 756-757 ◽  
Author(s):  
DAVID R. COLTHURST ◽  
CHRISTOPHER G. PROUD
Keyword(s):  
Protein Synthesis ◽  
Functional Properties ◽  
Rat Liver ◽  
Initiation Factors ◽  
Structural And Functional Properties ◽  
Protein Synthesis Initiation

scholarly journals Characterization of the ATP-dependent binding of wheat germ protein synthesis initiation factors eIF-(iso)4F and eIF-4A to mRNA.

1993 ◽  
Vol 268 (25) ◽  
pp. 18599-18603
Author(s):  
M.L. Balasta ◽  
S.E. Carberry ◽  
D.E. Friedland ◽  
R.A. Perez ◽  
D.J. Goss
Keyword(s):  
Protein Synthesis ◽  
Wheat Germ ◽  
Initiation Factors ◽  
Protein Synthesis Initiation

scholarly journals Differences in size, structure and function of free and membrane-bound polyribosomes of rat liver. Evidence for a single class of membrane-bound polyribosomes

1977 ◽  
Vol 168 (1) ◽  
pp. 1-8 ◽  
Author(s):  
J C Ramsey ◽  
W J Steele
Keyword(s):  
Protein Synthesis ◽  
Rat Liver ◽  
Size Structure ◽  
Large Fraction ◽  
Liver Homogenate ◽  
Structure And Function ◽  
Structural And Functional Properties ◽  
Membrane Bound ◽  
And Function

Free loosely bound and tightly bound polyribosomes were separated from rat liver homogenate by salt extraction followed by differential centrifugation, and several of their structural and functional properties were compared to resolve the existence of loosely bound polyribosomes and verify the specificity of the separation. The free and loosely bound polyribosomes have similar sedimentation profiles and polyribosome contents, their subunit proteins have similar electrophoretic patterns and their products of protein synthesis in vitro show a close correspondence in size and amounts synthesized. In contrast, the tightly bound polyribosomes have different properties from those of the free and loosely bound polyribosomes; their average size is significantly smaller; their polyribosome content is higher; their 60 S-subunit proteins lack two components and contain four or more components not found elsewhere; their products of protein synthesis in vitro differ in size and amounts synthesized. These observations show that rat liver membranes entrap a large fraction of the free polyribosomes at low salt concentrations and that these polyribosomes are similar to those of the free-polyribosome fraction and are different from those of the tightly bound polyribosome fraction in size, structure and function.

Modification of protein synthesis initiation factors and the shut-off of host protein synthesis in adenovirus-infected cells

Virology ◽  
1989 ◽  
Vol 168 (1) ◽  
pp. 112-118 ◽  
Author(s):  
Robert P. O'Malley ◽  
Roger F. Duncan ◽  
John W.B. Hershey ◽  
Michael B. Mathews
Keyword(s):  
Protein Synthesis ◽  
Host Protein ◽  
Initiation Factors ◽  
Infected Cells ◽  
Protein Synthesis Initiation ◽  
Host Protein Synthesis
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