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  • Title: Cloning, expression and characterization of theta-class glutathione S-transferase from the silkworm, Bombyx mori.
    Author: Yamamoto K, Zhang P, Miake F, Kashige N, Aso Y, Banno Y, Fujii H.
    Journal: Comp Biochem Physiol B Biochem Mol Biol; 2005 Jul; 141(3):340-6. PubMed ID: 15950511.
    Abstract:
    This study focused on glutathione S-transferase (GST), one of the detoxification enzymes, from the silkworm, Bombyx mori (GSTT1). A cDNA encoding a putative GST was amplified by reverse transcriptase-polymerase chain reaction and sequenced. The deduced amino acid sequence revealed 59%, 57% and 56% identities to theta-class GSTs of Musca domestica, Anopheles gambiae and Drosophila melanogaster, respectively. GSTT1 was also estimated to be close to those GSTs in a phylogenetic tree. Recombinant GST (rGSTT1) was functionally overexpressed in Escherichia coli in a soluble form, purified to homogeneity, and characterized. The pH-optimum of rGSTT1 was broad from pH 4 to 9 and rGSTT1 retained more than 75% of its original activity after incubation at pH 5-11. Incubation for 30 min at temperatures below 50 degrees C also affected the activity insignificantly. The Michaelis constant for 1-chloro-2,4-dinitrobenzene was 0.48 mM.
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