Studies on the relationship of hepatic anion-binding proteins and sulfobromophthalein-glutathione conjugation in normal and phenobarbital-treated rats.
The enzyme activity which conjugates sulfobromophthalein with glutathione was separated from rat liver supernate by Sephadex G-75 gel filtration, and assayed by two different methods; paper electrophoresis and spectrophotometry. The enzyme activity was found mainly in the second protein fraction, and less than 5% of the activity in the first or third protein fractions. In vitro mixtures of sulfobromophthalein, [3-H]glutathione and rat liver supernate showed that the major part of [3-H]glutathione was detected in the first and second protein fractions, and the remainder in the third protein fraction. Phenobarbital treatment caused an increase of the enzyme activity, sulfobromophthalein and [3-H]glutathione, in the second protein fraction.
D000818:Animals; D002850:Chromatography, Gel; D004798:Enzymes / Q000378:metabolism*; D005978:Glutathione / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D008297:Male; D010634:Phenobarbital / Q000494:pharmacology*; D011485:Protein Binding; D051381:Rats; D013448:Sulfobromophthalein / Q000378:metabolism*
D004798:Enzymes; D013448:Sulfobromophthalein; D005978:Glutathione; D010634:Phenobarbital