The Journal of Experimental Medicine, Vol 138, 483-487,
Copyright © 1973 by The Rockefeller University Press
ROLE OF HEPATIC ANION-BINDING PROTEIN IN BROMSULPHTHALEIN CONJUGATION
N. Kaplowitz 1,
I. W. Percy-Robb 1, and
N. B. Javitt 1
1 From the Gastroenterology Division, Cornell University Medical College, New York 10021
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.
Submitted on May 29, 1973