Identification of two lithocholic acid-binding proteins: Separation of ligandin from glutathione S-transferase B

J D Hayes, R C Strange, I W Percy-Robb

    Research output: Contribution to journalArticle

    71 Citations (Scopus)

    Abstract

    1. Two lithocholic acid-binding proteins in rat liver cytosol, previously shown to have glutathione S-transferase activity, were resolved by CM-Sephadex chromatography. 2. Phenobarbitone administration resulted in induction of both binding proteins. 3. The two proteins had distinct subunit compositions indicating that they are dimers with mol.wts. 44 000 and 47 000. 4. The two lithocholic acid-binding proteins were identified by comparing their elution volumes from CM-Sephadex with those of purified ligandin and glutathione S-transferase B prepared by published procedures. Ligandin and glutathione S-transferase B were eluted separately, as single peaks of enzyme activity, at volumes equivalent to the two lithocholic acid-binding proteins. 5. Peptide 'mapping' revealed structural differences between the two proteins.

    Original languageEnglish
    Pages (from-to)699-708
    Number of pages10
    JournalBiochemical Journal
    Volume181
    Issue number3
    Publication statusPublished - 1 Sep 1979

    Keywords

    • Animals
    • Carrier Proteins/biosynthesis
    • Chromatography, Ion Exchange
    • Cytosol/enzymology
    • Electrophoresis, Polyacrylamide Gel
    • Enzyme Induction
    • Glutathione Transferase/biosynthesis
    • Lithocholic Acid/metabolism
    • Liver/enzymology
    • Male
    • Peptide Fragments/analysis
    • Phenobarbital/pharmacology
    • Rats

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