2005年7月
Cloning, expression and characterization of theta-class glutathione S-transferase from the silkworm, Bombyx mori
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
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- 巻
- 141
- 号
- 3
- 開始ページ
- 340
- 終了ページ
- 346
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1016/j.cbpc.2005.04.012
- 出版者・発行元
- ELSEVIER SCIENCE INC
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 rGSTTI 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. (c) 2005 Elsevier Inc. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/j.cbpc.2005.04.012
- ISSN : 1096-4959
- Web of Science ID : WOS:000230613600012