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        검색결과 6

        1.
        2014.10 구독 인증기관·개인회원 무료
        Vitellogenins (Vgs) are precursors of the major egg storage protein, vitellin (Vn), in many oviparous animals. Insects Vgs are large molecules (200-kD) synthesized in the fat body in a process that involves substantial structural modifications (e.g., glycosylation, lipidation, phosphorylation, and proteolytic cleavage, etc.) of the nascent protein prior to its secretion and transport to the ovaries. However, the extent to which Vgs are processed in the fat body varies greatly among different insect groups. We were cloned Vgs partial genes PaVgs and BgVgs from Periplaneta americana and Blattella germanica. Real-time quantitative PCR shows that PaVgs and BgVgs were differential-regulated with aging. In insects, glutathione S-transferases (GSTs) are enzymes involved in detoxification of insecticides. We were cloned GST partial genes PaGST and BgGST from Periplaneta americana and Blattella germanica. Real-time quantitative PCR shows that PaGST and BgGST were up-regulated with aging, and the mRNA level of PaGST and BgGST was higher in 4℃ and 37℃ than room temperature. The expression level of PaGST and BgGST exposure to temperature stress suggests that PaGST and BgGST are up-regulated after exposure low and hige temperature treatments.
        2.
        2014.09 KCI 등재 구독 인증기관 무료, 개인회원 유료
        본 연구는 시험생물로서 말똥성게 (Hemicentrotus pulcherrimus) 를 이용하여 내분비계장애물질인 bisphenol A (BPA)의 독성 및 시험생물로서의 적합성 등을 조사하였 다. 말똥성게(H. pulcherrimus)의 수정 및 정상 배아발생 에 미치는 BPA의 독성을 보기 위하여 농도(0, 300, 500, 800, 1000, 1500 ppb)에서 조사하였다. BPA 노출 시 수정 률은 시험구간 내의 BPA 처리농도와 관계없이 유의적인 변화가 없었다. 정상 배아발생률은 BPA 농도가 높을수 록 유의적인 감소를 나타냈으며, 800 ppb 농도부터 유의 적인 감소를 보였다. 정상배아발생에 대한 독성값은 반 수영향농도 (EC50) 1056.1 ppb, 95% Cl 981.8~1163.9 ppb 로 나타났다. 또한 무영향농도 (NOEC)와 최소영향농도 (LOEC)는 500 ppb 및 800 ppb로 나타났다. BPA에 노출 된 배아는 농도가 증가함에 따라 발생이 정체되는 현상 이 나타났다. BPA에 노출된 pluteus 유생을 이용한 glutathione- S-transferase (GST) 유전자의 발현을 비교해본 결과 GST 유전자의 발현은 농도가 증가함에 따라 발현 이 증가하였다. 본 연구 결과, 말똥성게 (H. pulcherrimus)의 초기 배아 발생 과정 중 800 ppb 이상에서 독성을 나타냈으며 GST 유전자는 BPA 노출에 따른 위해성 평가에 생체지표유 전자로 유용하게 이용될 수 있다고 생각된다.
        4,000원
        3.
        2010.06 KCI 등재 구독 인증기관 무료, 개인회원 유료
        The effects of different dietary fatty acids on the hepatic glutathione S-transferase(GST-P) positive foci and glutathione related enzyme system were investigated in carcinogen treated rats. Weaning male Sprague Dawley rats were divided into three groups and fed the diets of 15% corn(CO), perilla(PO), and sardine oil(SO), respectively. Hepatocellular carcinogenesis was initiated with diethylnitrosamine(DEN) and then fed the diet containing 0.02% 2-acetylaminoflumene(2-AAF) followed by 0.05% phenobarbital for 10 weeks. The hepatic tissues were homogenized and centrifugated to prepare microsoma1 and cytosolic fractions. The enzyme activities of hepatic glutathione S-transferase(GST), glutathione reductase(GR), and glutathione peroxidase(GPx) were determined from cytosoIic Mans. The number of GST-P hyperplastic nodules was the highest in corn oil group at 6th week, the early stage of hyperplastic nodule formation. GST activities were increased significantly by carcinogens in a11 dietary groups after 6th wk. GR activities followed the same tread as GST activities. GPx activities were decreased by carcinogens in all dietary groups at 10th week. In this experiment, corn oil diet may have promotive effect on hyperplastic nodule formation during the early promotional stages of chemical carcinogenesis.
        4,000원
        5.
        2002.11 KCI 등재 서비스 종료(열람 제한)
        A gene coding for the GST of cotton (Gh-5) was cloned into Escherichia coli and experssed. The enzyme remained within the cytoplasm of E. coli. An 696 bp open reading frame was in the 988 base pair fragment of the recombinant plasmid pET-30b(+). The deduced protein sequence consists of 232 amino acids and has a molecular mass of 30235.58 Da. The cloned enzyme conjugated reduced glutathione and 1-chloro-2,4-dinitrobenzene (CDNB). Plant GST cDNA was expressed in microbe and produced polypeptide had function as an enzyme.