Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 신경훈 | - |
dc.date.accessioned | 2019-07-15T06:45:52Z | - |
dc.date.available | 2019-07-15T06:45:52Z | - |
dc.date.issued | 2007-11 | - |
dc.identifier.citation | COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY, v. 146, No. 4, Page. 471-477 | en_US |
dc.identifier.issn | 1532-0456 | - |
dc.identifier.issn | 1878-1659 | - |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S153204560700138X | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/107395 | - |
dc.description.abstract | We 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.sponsorship | This 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.iso | en_US | en_US |
dc.publisher | ELSEVIER SCIENCE INC | en_US |
dc.subject | polychaete | en_US |
dc.subject | Neanthes succinea | en_US |
dc.subject | glutathione S-transferases | en_US |
dc.subject | antioxidant defense | en_US |
dc.subject | biomarker | en_US |
dc.title | Molecular 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.type | Article | en_US |
dc.identifier.doi | 10.1016/j.cbpc.2007.05.003 | - |
dc.relation.journal | COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY | - |
dc.contributor.googleauthor | Rhee, Jae-Sung | - |
dc.contributor.googleauthor | Lee, Young-Mi | - |
dc.contributor.googleauthor | Hwang, Dae-Sik | - |
dc.contributor.googleauthor | Lee, Kyun-Woo | - |
dc.contributor.googleauthor | Kim, Il-Chan | - |
dc.contributor.googleauthor | Shin, Kyung-Hoon | - |
dc.contributor.googleauthor | Raisuddin, Sheikh | - |
dc.contributor.googleauthor | Lee, Jae-Seong | - |
dc.relation.code | 2007212665 | - |
dc.sector.campus | E | - |
dc.sector.daehak | COLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY[E] | - |
dc.sector.department | DEPARTMENT OF MARINE SCIENCE AND CONVERGENCE ENGINEERING | - |
dc.identifier.pid | shinkh | - |
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