Characterization of bovine phenol sulfotransferases: evidence of a major role for SULT1B1 in the liver

Kanika V. Choughule, Charles W. Locuson, Michael W. H. Coughtrie (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    2 Citations (Scopus)


    1. Cattle are an important component of the human food chain. Drugs used either legally or illegally in cattle may therefore enter the food chain and it is thus important to understand pathways of drug metabolism in this species, including sulfation catalyzed by the sulfotransferases (SULTs).

    2. In this study, we have analyzed the sulfation of 4-nitrophenol and other compounds in male and female bovine liver and characterized recombinant bovine SULT isoforms 1A1 and 1B1 expressed in Escherichia coli.

    3. We found that, in contrast to most other mammalian species, the major phenol sulfotransferase SULT1A1 is not expressed in bovine liver. Rather SULT1B1 seems to be a major form in both male and female bovine liver.

    4. We also identified kinetic differences between bovine and human SULT1A1 and, using the human SULT1A1 crystal structure, identified two amino acid positions in the active site of bovine SULT1A1 (Ile89Val and Phe247Val) that may be responsible for these differences.

    Original languageEnglish
    Pages (from-to)495-502
    Number of pages8
    Issue number6
    Publication statusPublished - 2015


    • Cattle
    • Liver
    • Sulfotransferase
    • SULT1A1
    • SULT1B1

    ASJC Scopus subject areas

    • Pharmacology
    • Toxicology
    • Biochemistry
    • Health, Toxicology and Mutagenesis


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