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Abstract Based on the EST sequence of Glutathione S-transferase gene (TaGST) from Tamarix androssowii published on GenBank, a TaGST cDNA was cloned with 3’and 5’RACE techniques. The full length of TaGST is 1175 bp with ORF of 672 bp deduced 224 amino acid residues. The deduced amino acid sequence encoded by TaGST is homologous with that of known plant GST and the highest identity is 48% (GST10 of Glycine max). To characterize its function, the TaGST expression vector was constructed with pET-28a(+) and transformed into E. coli BL21. The SDS-PAGE result showed that the TaGST protein was expressed and the molecular weight was about 26 kD which is similar to the caculated one’s. The enzyme activity assay of the TaGST indicated that TaGST could catalyze the substrate reaction of CDNB with GSH. This confirmed that the TaGST did encode a functional GST protein.
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Received: 31 March 2006
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