title: Role of hepatic anion-binding protein in bromsulphthalein conjugation.
abstract: Using gel filtration, the binding of both glutathione and Bromsulphthalein (BSP) to a liver-soluble protein was found to be identical. BSP-conjugating activity (glutathione S-aryltransferase) was present only in the fractions corresponding to the two protein-bound markers. Using a highly sensitive assay, with 3,4-dichloronitrobenzene, the pattern of glutathione S-aryltransferase activity was found to coincide with Y protein. This evidence suggests that Y protein, or ligandin, has a dual role in hepatic transport: a specific enzymic function in the conjugation of certain anions with glutathione in addition to a transport function in the intracellular binding of organic anions.
mesh_terms: D000818:Animals; D001692:Biological Transport; D002850:Chromatography, Gel; D005978:Glutathione / Q000378:metabolism; D008099:Liver / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D013448:Sulfobromophthalein / Q000378:metabolism*; D014316:Tritium
chemical_list: D013448:Sulfobromophthalein; D014316:Tritium; D005978:Glutathione