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dc.contributor.author신경훈-
dc.date.accessioned2019-07-15T06:45:52Z-
dc.date.available2019-07-15T06:45:52Z-
dc.date.issued2007-11-
dc.identifier.citationCOMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY, v. 146, No. 4, Page. 471-477en_US
dc.identifier.issn1532-0456-
dc.identifier.issn1878-1659-
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S153204560700138X-
dc.identifier.urihttp://repository.hanyang.ac.kr/handle/20.500.11754/107395-
dc.description.abstractWe cloned and sequenced a full-length cDNA of an omega class glutathione S-transferase (GST-O) from the polychaete Neanthes succinea (ns-GST-O). The full-length cDNA of ns-GST-O was 1562 bp in length, containing an open reading frame (OR) of 732 bp that encoded a 244 amino acid protein. The deduced amino acid sequence of ns-GST-O showed a low similarity with the theta class N. suucinea GST (ns-GST-T). As GSTs play a significant role in antioxidant defense, we checked the expression pattern of ns-GST-0 in N. succinea after exposure to copper (CUCl2 12 to 72 mu g/L), which is an oxidative stress-inducing agent. After exposure to CUCl2, ns-GST-O gene was dramatically up-regulated and when compared with ns-GST-T the expression pattern was more pronounced at all the concentrations of copper. Even the basal transcription levels of ns-GST-O were higher than those of ns-GST-T To further characterize the catalytic properties of ns-GST-O, we constructed a recombinant ns-GST-O plasmid with a 6x His-Tag at the N-terminal of the full-length ns-GST-O cDNA. Recombinant ns-GST-O protein was highly expressed in transformed Escherichia coli. The effect of pH, temperature and chemical inhibitors on the enzyme activity of ns-GST-O was also studied and compared with the reported effect of these factors on recombinant ns-GST-T protein. These results suggest that, like other types of GSTs, ns-GST-O protein plays a conserved antioxidant role in the polychacte N. succinea. (C) 2007 Elsevier Inc. All rights reserved.en_US
dc.description.sponsorshipThis work was supported by a National Research Lab (NRL) grant (R0A-2006-000-10155-0) of the Korea Science and Engineering Foundation (KOSEF) funded to Jae-Seong Lee.en_US
dc.language.isoen_USen_US
dc.publisherELSEVIER SCIENCE INCen_US
dc.subjectpolychaeteen_US
dc.subjectNeanthes succineaen_US
dc.subjectglutathione S-transferasesen_US
dc.subjectantioxidant defenseen_US
dc.subjectbiomarkeren_US
dc.titleMolecular cloning and characterization of omega class glutathione S-transferase (GST-O) from the polychaete Neanthes succinea: Biochemical comparison with theta class glutathione S-transferase (GST-T)en_US
dc.typeArticleen_US
dc.identifier.doi10.1016/j.cbpc.2007.05.003-
dc.relation.journalCOMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY-
dc.contributor.googleauthorRhee, Jae-Sung-
dc.contributor.googleauthorLee, Young-Mi-
dc.contributor.googleauthorHwang, Dae-Sik-
dc.contributor.googleauthorLee, Kyun-Woo-
dc.contributor.googleauthorKim, Il-Chan-
dc.contributor.googleauthorShin, Kyung-Hoon-
dc.contributor.googleauthorRaisuddin, Sheikh-
dc.contributor.googleauthorLee, Jae-Seong-
dc.relation.code2007212665-
dc.sector.campusE-
dc.sector.daehakCOLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY[E]-
dc.sector.departmentDEPARTMENT OF MARINE SCIENCE AND CONVERGENCE ENGINEERING-
dc.identifier.pidshinkh-


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