کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1977992 | 1061521 | 2009 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Biochemical properties of an omega-class glutathione S-transferase of the silkmoth, Bombyx mori Biochemical properties of an omega-class glutathione S-transferase of the silkmoth, Bombyx mori](/preview/png/1977992.png)
A cDNA encoding an omega-class glutathione S-transferase of the silkmoth, Bombyx mori (bmGSTO), was cloned by reverse transcriptase-polymerase chain reaction. The resulting clone was sequenced and deduced for amino acid sequence, which revealed 40, 40, and 39% identities to omega-class GSTs from human, pig, and mouse, respectively. A recombinant protein (rbmGSTO) was functionally overexpressed in Escherichia coli cells in a soluble form and purified to homogeneity. rbmGSTO was able to catalyze the biotranslation of glutathione with 1-chloro-2,4-dinitrobenzene, a model substrate for GST, as well as with 4-hydroxynonenal, a product of lipid peroxidation. This enzyme was shown to have high affinity for organophosphorus insecticide and was present abundantly in silkmoth strain exhibiting fenitrothion resistance. These results indicate that bmGSTO could be involved in the increase in level of insecticide resistance for lepidopteran insects.
Journal: Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology - Volume 149, Issue 4, May 2009, Pages 461–467