The Rat Liver GlutathioneS-Transferase Ya Subunit Gene:  Characterization of the Binding Properties of a Nuclear Protein from HepG2 Cells That Has High Affinity for the Antioxidant Response Element

Biochemistry ◽  
1996 ◽  
Vol 35 (35) ◽  
pp. 11517-11521 ◽  
Author(s):  
Suxing Liu ◽  
Cecil B. Pickett
Keyword(s):  
Rat Liver ◽  
Hepg2 Cells ◽  
Nuclear Protein ◽  
Antioxidant Response ◽  
Antioxidant Response Element ◽  
Subunit Gene ◽  
Binding Properties ◽  
Gene Characterization ◽  
High Affinity

scholarly journals Characterization of solubilized insulin receptors from rat liver microsomes. Existence of two receptor species with different binding properties

1986 ◽  
Vol 154 (2) ◽  
pp. 281-287 ◽  
Author(s):  
Rudiger KOCH ◽  
Arno DEGER ◽  
Hans-Martin JACK ◽  
Karl-Norbert KLOTZ ◽  
Dieter SCHENZLE ◽  
...  
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Insulin Receptors ◽  
Rat Liver Microsomes ◽  
Binding Properties

scholarly journals Isolation and characterization of membrane proteins responsible for attachment of polyribosomes to rough microsomal fraction of rat liver

1977 ◽  
Vol 164 (1) ◽  
pp. 53-66 ◽  
Author(s):  
S Fujita ◽  
F Ogata ◽  
J Nakamura ◽  
S Omata ◽  
H Sugano
Keyword(s):  
Rat Liver ◽  
Protein Fraction ◽  
Microsomal Fraction ◽  
Binding Capacity ◽  
Gel Filtration ◽  
High Affinity ◽  
Isolation And Characterization ◽  
Microsomal Membranes ◽  
Equilibrium Centrifugation

A protein fraction which has a high affinity for polyribosomes was isolated from rough microsomal membranes of rat liver. The mode of polyribosome binding to this fraction (R-fraction) was studied by using CsCl equilibrium centrifugation and compared with that for stripped rough microsomal membranes. The following were found. (1) The polyribosome-binding cpacity of the R-fraction was heat-labile and sensitive to trypsin, and was suppressed by increasing KCl concentration and addition of 0.1 mM-aurintricarboxylic acid. (2) Of the four subfractions obtained by gel filtration of the R-fraction on a Sephadex G-200, only the R1-fraction, eluted at the void volume, showed a high affinity for polyribosomes. The polyribosome-binding capacity of the R1-fraction decreased with time on storage at 4 degrees C. (3) The R1-fraction contained three major proteins with mol. wts. 108,000, 99,000 and 65,000.

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