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Expression and characterization of a recombinant Drosophila tyramine-${eta}$-hydroxylase in silkworm infected with recombinant baculovirus
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  • Expression and characterization of a recombinant Drosophila tyramine-${eta}$-hydroxylase in silkworm infected with recombinant baculovirus
  • Expression and characterization of a recombinant Drosophila tyramine-${eta}$-hydroxylase in silkworm infected with recombinant baculovirus
저자명
Ali. Ahmed M.H.,Lee. Jae Man,Yoshida. Mayumi,Sakashita. Kosuke,Torii. Jumpei,Kusakabe. Takahiro,Hirashima. Akinori
간행물명
Journal of Asia-Pacific entomology
권/호정보
2012년|15권 4호|pp.567-572 (6 pages)
발행정보
한국응용곤충학회
파일정보
정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

The insect nervous system contains biogenic amines such octopamine (OA),which is synthesized from tyramine (TA) by catalysis of tyramine-${eta}$-hydroxylase ($T{eta}H$). In this study, the Drosophila 70 kDa tyramine-${eta}$-hydroxylase ($DmT{eta}H$) protein was purified after the recombinant nucleopolyhedrovirus isolated from Bombyx mori (BmNPV) containing the $T{eta}H$ gene was injected into the hemocoel of the fifth instar larvae from the d17 B. mori strain. Western blot analysis revealed an immunoreactive band with a molecular mass of 70 kDa. The products formed by incubating the enzyme reaction mixture were separated and detected by reverse phase high-performance liquid chromatography. The optimum pH, temperature, and incubation time for the conversion of TA to OA were 7.6, $25^{circ}C$, and 30 min, respectively. The inhibitory experiments using various concentrations of 1-(2-methoxy-5-methylphenyl) imidazole-2(3H)-thione (MMIT) showed that MMIT inhibited $DmT{eta}H$ dose-dependently and that this method can be applied for screening $DmT{eta}H$ inhibitors.