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- W2067331012 abstract "Abstract Isolation of glutathione S- transferase from the New Zealand grass grub, is complicated by the marked loss of activity from crude homogenates. This loss may be due to proteolysis or to modification by endogenous chemicals. The effect may be minimized by immediate fractionation with ammonium sulphate and by inclusion of 5mM glutathione in homogenates. Two enzymes species, isoelectric at pH 8.7 and 5.9 respectively, could be isolated by ammonium sulphate fractionation, affinity chromatography, anion exchange chromatography and chromatography on hydroxyl apatite. They had different substrate specificities and had differing subunit structure. The pI 8.7 enzyme appeared to be a homodimer of subunits of M r 23,700 and the pI 5.9 enzyme one of subunit M r 22,500. A third major enzyme species, isoelectric at pH 4.3 differed from the other two enzymes in having low affinity for the affinity matrix. This preparation was heterogeneous. The enzymically active species in this preparation had the same molecular weight as that of the pI 8.7 enzyme, had a very similar substrate specificity to the basic enzyme species and was characterized by kinetic parameters almost identical to those of the pI 8.7 enzyme." @default.
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- W2067331012 date "1985-01-01" @default.
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- W2067331012 title "Glutathione from the New Zealand grass grub, Costelytra zealandica Their isolation and characterization and the effect on their activity of endogenous factors" @default.
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- W2067331012 doi "https://doi.org/10.1016/0020-1790(85)90041-1" @default.
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