Study summary · research use only
The glutathione S-transferases of fish
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
This review describes glutathione S-transferase activity and reduced glutathione (GSH) in tissues of fish (teleosts and elasmobranchs). The abstract reports that hepatic fish enzymes conjugate a range of electrophilic substrates with GSH, with narrower specificities than rodent liver transferases, and that no good evidence was found for ligandin-like or 'suicide' functions. It states all fish livers tested had several transferase isoenzymes, dimers of subunits of about 25 kDa with possibly different catalytic properties, and that in some species activity is induced by agents such as phenols or 3-methylcholanthrene.
Abstract
Substantial soluble glutathione S-transferase activity and millimolar reduced glutathione (GSH) are present in most tissues of both teleosts and elasmobranchs. The hepatic enzymes of fish conjugate a range of electrophilic substrates with GSH, although their specificities are less broad than those of the transferases in rodent liver. There is no good evidence that fish transferases have ligandin-like activity or a 'suicide' function. All fish livers tested have several transferase isoenzymes. They are dimers of subunits whose Mrs are about 25 kDa and which may have different catalytic properties. In some species transferase activity is induced by agents such as phenols or 3-methylcholanthrene. Glutathione S-transferases are important detoxication enzymes in fish.
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