Glutathione S-transferase from an antarctic fish, Dissostichus mawsoni

Glutathione S-transferase activity was measured in the hepatic cytosol front Dissostichus mawsoni and Pagothenia borchgrevinki. Activity measures with 1-chloro-2,4-dinitrobenzene as substrate were 11·2 and 16·7 μmol/min/g tissue respectively. Little or no activity was detected when p-nitrobenzyl chloride or 3,4-dichloro-1-nitrobenzene were used as substrate. The hepatic glutathione S-transferases from D. mawsoni were partially purified using gel filtration and chromatofocusing. Three peaks of activity were resolved. The major isozyme (158-fold purification) eluting at pH7·1 appeared to be catalytically a homodimer. The isozyme was highly inhibited by triphenyltin chloride (IC₅₀ = 0·1 μ) while inhibition constants for Cibicron Blue 3GA, bromosulphophalein and hematin were 1·1, 20 and 34 μ respectively.