Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10820501 | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology | 2005 | 7 Pages |
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 °C also affected the activity insignificantly. The Michaelis constant for 1-chloro-2,4-dinitrobenzene was 0.48 mM.
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Authors
Kohji Yamamoto, Pingbo Zhang, Fumio Miake, Nobuhiro Kashige, Yoichi Aso, Yutaka Banno, Hiroshi Fujii,