AI Article Synopsis
- Cattle play a crucial role in the food chain, making it essential to study how drugs metabolize in them, particularly through sulfation by sulfotransferases (SULTs).
- In this research, the sulfation processes of certain compounds were examined in male and female bovine liver, focusing on recombinant bovine SULT isoforms 1A1 and 1B1.
- Unlike most mammals, bovine liver lacks the major phenol sulfotransferase SULT1A1, with SULT1B1 being prevalent instead, and distinct kinetic differences were found between bovine and human SULT1A1, linked to specific amino acid variations.
Article Abstract
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.
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| http://dx.doi.org/10.3109/00498254.2014.997325 | DOI Listing |
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