Purification with hydrophobic interaction chromatography and properties of two bilirubin-binding proteins and other glutathione S-transferases from rat liver cytosol

1981 ◽  
Vol 9 (4) ◽  
pp. 302-303 ◽  
Author(s):  
JULES A. T. P. MEUWISSEN ◽  
MARCEL ZEEGERS
Keyword(s):  
Rat Liver ◽  
Hydrophobic Interaction ◽  
Binding Proteins ◽  
Hydrophobic Interaction Chromatography ◽  
Liver Cytosol ◽  
Glutathione S Transferases ◽  
Bilirubin Binding ◽  
Rat Liver Cytosol

Effect of Glutathione on the Activity of Bilirubin-Binding Proteins from Rat Liver Cytosol

1977 ◽  
Vol 5 (5) ◽  
pp. 1404-1407 ◽  
Author(s):  
JULES A. T. P. MEUWISSEN ◽  
MARCEL ZEEGERS ◽  
KAILA SINGH SRAI ◽  
BRIAN KETTERER
Keyword(s):  
Rat Liver ◽  
Binding Proteins ◽  
Liver Cytosol ◽  
Bilirubin Binding ◽  
Rat Liver Cytosol

Triiodothyronine binding proteins in rat liver cytosol

1975 ◽  
Vol 67 (3) ◽  
pp. 995-1004 ◽  
Author(s):  
N. Defer ◽  
B. Dastugue ◽  
M.M. Sabatier ◽  
P. Thomopoulos ◽  
J. Kruh
Keyword(s):  
Rat Liver ◽  
Binding Proteins ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Glucocorticoid-binding Proteins of Rat Liver Cytosol

1972 ◽  
Vol 247 (24) ◽  
pp. 7890-7896
Author(s):  
Miguel Beato ◽  
Philip Feigelson
Keyword(s):  
Rat Liver ◽  
Binding Proteins ◽  
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.

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