A comparison of the subcellular distribution, subunit composition and bile acid-binding activity of glutathione S-transferases from trout and rat liver

1981 ◽  
Vol 68 (4) ◽  
pp. 579-584 ◽  
Author(s):  
I.A. Nimmo ◽  
D.R. Coghill ◽  
J.D. Hayes ◽  
R.C. Strange
Keyword(s):  
Bile Acid ◽  
Rat Liver ◽  
Subcellular Distribution ◽  
Binding Activity ◽  
Subunit Composition ◽  
Glutathione S Transferases ◽  
Bile Acid Binding

scholarly journals Studies on the subunit composition of rat liver glutathione S-transferases.

1983 ◽  
Vol 258 (18) ◽  
pp. 11321-11325 ◽  
Author(s):  
A B Frey ◽  
T Friedberg ◽  
F Oesch ◽  
G Kreibich
Keyword(s):  
Rat Liver ◽  
Subunit Composition ◽  
Liver Glutathione ◽  
Glutathione S Transferases

Subunit composition of rat liver glutathione S-transferases

1982 ◽  
Vol 108 (2) ◽  
pp. 461-467 ◽  
Author(s):  
Chen-Pei D. Tu ◽  
Mitchell J. Weiss ◽  
C. Channa Reddy
Keyword(s):  
Rat Liver ◽  
Subunit Composition ◽  
Liver Glutathione ◽  
Glutathione S Transferases

Stability, antioxidant activity and in vitro bile acid-binding of green, black and dark tea polyphenols during simulated in vitro gastrointestinal digestion

RSC Advances ◽  
2015 ◽  
Vol 5 (112) ◽  
pp. 92089-92095 ◽  
Author(s):  
Zhengmei Wu ◽  
Jianwen Teng ◽  
Li Huang ◽  
Ning Xia ◽  
Baoyao Wei
Keyword(s):  
Antioxidant Activity ◽  
Bile Acid ◽  
Phenolic Compounds ◽  
Binding Activity ◽  
Tea Polyphenols ◽  
Gastrointestinal Digestion ◽  
In Vitro Gastrointestinal Digestion ◽  
Bile Acid Binding ◽  
The Stability

The stability and antioxidant activity of phenolic compounds, as well as the bile acid-binding activity of green, black, raw liubao and aged liubao tea duringin vitrogastrointestinal digestion were evaluated.

scholarly journals Ability of chicken protein hydrolysate to lower serum cholesterol through its bile acid binding activity

2020 ◽  
Vol 18 (1) ◽  
pp. 493-499
Author(s):  
Pei-Ting Wu ◽  
Yie-Qie Lau ◽  
Fan-Jhen Dai ◽  
Jia-Ting Lin ◽  
Hung-Yuan Kao ◽  
...  
Keyword(s):  
Bile Acid ◽  
Serum Cholesterol ◽  
Protein Hydrolysate ◽  
Binding Activity ◽  
Lower Serum ◽  
Lower Serum Cholesterol ◽  
Bile Acid Binding ◽  
Chicken Protein

Comparison of bile acid binding to sinusoidal and bile canalicular membranes isolated from rat liver

1987 ◽  
Vol 901 (1) ◽  
pp. 15-22 ◽  
Author(s):  
Kiyoto Yachi ◽  
Yuichi Sugiyama ◽  
Tatsuji Iga ◽  
Yusei Ikeda ◽  
Gotaro Toda ◽  
...  
Keyword(s):  
Bile Acid ◽  
Rat Liver ◽  
Bile Acid Binding

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 Cholic acid binding by glutathione S-transferases from rat liver cytosol

1980 ◽  
Vol 185 (1) ◽  
pp. 83-87 ◽  
Author(s):  
J D Hayes ◽  
R C Strange ◽  
I W Percy-Robb
Keyword(s):  
Bile Acid ◽  
Cholic Acid ◽  
Reduced Glutathione ◽  
Binding Activity ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Liver Cytosol ◽  
Glutathione S Transferases ◽  
Rat Livers ◽  
Rat Liver Cytosol

Cholic acid-binding activity in cytosol from rat livers appears to be mainly associated with enzymes having glutathione S-transferase activity; at least four of the enzymes in this group can bind the bile acid. Examination of the subunit compositions of different glutathione S-transferases indicated that cholic acid binding and the ability to conjugate reduced glutathione with 1,2-dichloro-4-nitrobenzene may be ascribed to different subunits.

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