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PMID: 4719680 Published · ppublish English Journal Article

Role of hepatic anion-binding protein in bromsulphthalein conjugation.

The Journal of experimental medicine ·Vol. 138 ·No. 2 ·1973-08-01 ·Pages 483-7

Kaplowitz N, Percy-Robb IW, Javitt NB

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
Animals Biological Transport Chromatography, Gel Glutathione/metabolism Liver/metabolism Protein Binding Rats Sulfobromophthalein/metabolism Tritium
Chemicals
Sulfobromophthalein Tritium Glutathione
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kaplowitz N
Percy-Robb I W
Javitt N B
References (10)
10 references, click to expand
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    J Clin Invest. 1960 Oct;39:1570-7 PMID: 13789668
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Article Info
Journal
The Journal of experimental medicine
Abbr.
J Exp Med
ISSN
0022-1007
Published
1973-08-01
Pages
483-7
Language
English
Region
United States
NLM ID
2985109R
PMCID
PMC2139406
Subset
IM
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