Studies on the relationship between glutathione S-transferase phenotype and bile acid binding by human liver cytosol.
The possibility that the GST1 phenotype of human liver cytosol is a determinant of bile salt binding has been investigated by using equilibrium dialysis and gel-exclusion chromatography. Binding of bile salts was non-saturable and whereas the glutathione S-transferases did not appear to be major bile salt binders, other binding components with molecular weights of 35 000 and 11 000 were identified in both fetal and adult cytosols.
D000328:Adult; D000818:Animals; D001647:Bile Acids and Salts / Q000378:metabolism*; D002850:Chromatography, Gel; D003593:Cytoplasm / Q000201:enzymology / Q000378:metabolism; D005260:Female; D005333:Fetus / Q000378:metabolism; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism*; D006000:Glycocholic Acid / Q000378:metabolism; D006801:Humans; D007231:Infant, Newborn; D007234:Infant, Premature; D008095:Lithocholic Acid / Q000378:metabolism; D008099:Liver / Q000201:enzymology / Q000378:metabolism*; D008970:Molecular Weight; D010641:Phenotype; D011247:Pregnancy; D051381:Rats
D001647:Bile Acids and Salts; D008095:Lithocholic Acid; D005982:Glutathione Transferase; D006000:Glycocholic Acid