Abstract
AbstractActive glutathione S‐transferase (GST) has been purified from needles of Norway spruce (Picea abies L. Karst.). Two isoforms of the enzyme which exhibit different physico‐chemical and catalytic properties were separated by (NH4)2SO4 fractionation, affinity chromatography on epoxy‐activated 4% cross‐linked beaded agarose, using glutathione as the ligand, ion‐exchange chromatography, and isoelectric focusing. The isozymes have pI values of 5.5 (GST I) and 4.3 (GST II). Both GST isozymes are homodimeric proteins with subunit sizes of 26 kD (GST I), and 23 kD (GST II). The kinetic properties of the enzymes are described and compared with other plants GSTs. Only GST II is able to conjugate the pesticides fluorodifen and alachlor.
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