scholarly journals RNA Binding Activity Induced by TCDD in Rat Liver Cytosol(PROCEEDINGS OF 24TH SYMPOSIUM ON TOXICOLOGY AND ENVIRONMENTAL HEALTH)

1999 ◽  
Vol 45 (1) ◽  
pp. P6-6
Author(s):  
Shigeki Shimba ◽  
Hideko Sone ◽  
Junzo Yonemoto ◽  
Masakatsu Tezuka
Keyword(s):  
Environmental Health ◽  
Rat Liver ◽  
Rna Binding ◽  
Binding Activity ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals A study of the structures of the YaYa and YaYc glutathione S-transferases from rat liver cytosol Evidence that the Ya monomer is responsible for lithocholate-binding activity

1981 ◽  
Vol 197 (2) ◽  
pp. 491-502 ◽  
Author(s):  
J D Hayes ◽  
R C Strange ◽  
I W Percy-Robb
Keyword(s):  
Rat Liver ◽  
Lithocholic Acid ◽  
Binding Activity ◽  
Glutathione S Transferase ◽  
Liver Cytosol ◽  
Molecular Weights ◽  
Tryptic Digest ◽  
Glutathione S Transferases ◽  
Limited Digestion ◽  
Rat Liver Cytosol

The two dimeric lithocholic acid-binding proteins previously identified as ligandin (YaYa) and glutathione S-transferase B (YaYc) were isolated from rat liver cytosol. These proteins have molecular weights of 44000 and 47000 respectively. The recovery of these two proteins from liver was not affected by the addition of the proteinase inhibitor Trasylol. No spontaneous interconversion between these two proteins was observed on storage. YaYa and YaYc proteins yielded peptides of identical molecular weight after limited digestion with Staphylococcus aureus V8 proteinase. Analytical and preparative tryptic-digest peptide ‘maps’ showed that all the soluble peptides obtained from YaYa protein were also recovered from YaYc protein. Approximately six extra soluble peptides, which were not recovered from YaYa protein, were obtained from the tryptic digest of YaYc protein. Subdigests of the insoluble tryptic-digest ‘cores’ also resulted in the recovery of identical peptides from both proteins. Evidence is presented that the Ya subunit possessed by both proteins is identical; glutathione S transferase B is a hybrid of ligandin and glutathione S-transferase AA. The Ya monomer is responsible for lithocholate binding.

scholarly journals Alterations in translatable messenger RNA coding for phosphoenolpyruvate carboxykinase (GTP) in rat liver cytosol during deinduction.

1978 ◽  
Vol 253 (12) ◽  
pp. 4327-4332
Author(s):  
D. Kioussis ◽  
L. Reshef ◽  
H. Cohen ◽  
S.M. Tilghman ◽  
P.B. Iynedjian ◽  
...  
Keyword(s):  
Rat Liver ◽  
Messenger Rna ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Transformation of the glucocorticoid receptor in rat liver cytosol by lysosomal enzymes.

1979 ◽  
Vol 254 (5) ◽  
pp. 1537-1539 ◽  
Author(s):  
J. Carlstedt-Duke ◽  
O. Wrange ◽  
E. Dahlberg ◽  
J.A. Gustafsson ◽  
B. Högberg
Keyword(s):  
Glucocorticoid Receptor ◽  
Rat Liver ◽  
Lysosomal Enzymes ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

Development of an [3H] glucocorticoid exchange assay in rat liver cytosol

Steroids ◽  
1981 ◽  
Vol 37 (4) ◽  
pp. 409-421 ◽  
Author(s):  
Ashutosh Banerji ◽  
Mohammed Kalimi
Keyword(s):  
Rat Liver ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Rat liver cytosol oxysterol-binding protein

FEBS Letters ◽  
1987 ◽  
Vol 210 (1) ◽  
pp. 97-103 ◽  
Author(s):  
F. Beseme ◽  
M.E. Astruc ◽  
R. Defay ◽  
A.Crastes de Paulet
Keyword(s):  
Rat Liver ◽  
Binding Protein ◽  
Liver Cytosol ◽  
Oxysterol Binding Protein ◽  
Rat Liver Cytosol
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