Cloning and expression of glutathione S-transferase(GST) cDNA from Gossypium hirsutum L.
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A gene coding for the GST of cotton (Gh-5) was cloned into Escherichia coli and experessed. The enzyme remained within the cytoplasm of E. coli. An 696 bp open reading frame was in the 988 base pair fragment of the recombinant plasmid pET-30b(+). The deduced protein sequence consists of 232 amino acids and has a molecula mass of 30235.58 Da. The cloned enzyme conjugated reduced glutathione and lchloro-2,4-dinitrobenzene (CDNB). Plant GST cDNA was expressed in microbe and produced polyeptide had function as an enzyme.
Abstract
A gene coding for the GST of cotton (Gh-5) was cloned into Escherichia coli and experessed. The enzyme remained within the cytoplasm of E. coli. An 696 bp open reading frame was in the 988 base pair fragment of the recombinant plasmid pET-30b(+). The deduced protein sequence consists of 232 amino acids and has a molecula mass of 30235.58 Da. The cloned enzyme conjugated reduced glutathione and lchloro-2,4-dinitrobenzene (CDNB). Plant GST cDNA was expressed in microbe and produced polyeptide had function as an enzyme.