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- Publisher Website: 10.1016/j.febslet.2005.05.070
- Scopus: eid_2-s2.0-21244500981
- PMID: 15967446
- WOS: WOS:000230335600046
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Article: Seabream antiquitin: Molecular cloning, tissue distribution, subcellular localization and functional expression
Title | Seabream antiquitin: Molecular cloning, tissue distribution, subcellular localization and functional expression |
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Authors | |
Keywords | Aldehyde dehydrogenase Antiquitin ALDH7A1 Tissue distribution Subcellular localization Eukaryotic expression |
Issue Date | 2005 |
Citation | FEBS Letters, 2005, v. 579, n. 17, p. 3759-3764 How to Cite? |
Abstract | Subsequent to our earlier report on the first purification of antiquitin protein from seabream liver and demonstration of its enzymatic activity [FEBS Letters 516 (2002) 183-186], we report herein the cloning of its full-length cDNA sequence. The open reading frame encodes a protein of 511 amino acids. Results of RT-PCR indicate that antiquitin is highly expressed in both the seabream liver and kidney. Transfection studies in cultured eukaryotic cells provided further evidence that it is a cytosolic protein. Bacterial expression of the enzyme was also performed. The purified recombinant protein was demonstrated to exhibit similar kinetic properties as the native enzyme. © 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
Persistent Identifier | http://hdl.handle.net/10722/225024 |
ISSN | 2023 Impact Factor: 3.0 2023 SCImago Journal Rankings: 1.208 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Tang, Wai Kwan | - |
dc.contributor.author | Chan, Chi Bun | - |
dc.contributor.author | Cheng, Christopher H K | - |
dc.contributor.author | Fong, Wing Ping | - |
dc.date.accessioned | 2016-04-18T11:16:32Z | - |
dc.date.available | 2016-04-18T11:16:32Z | - |
dc.date.issued | 2005 | - |
dc.identifier.citation | FEBS Letters, 2005, v. 579, n. 17, p. 3759-3764 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | http://hdl.handle.net/10722/225024 | - |
dc.description.abstract | Subsequent to our earlier report on the first purification of antiquitin protein from seabream liver and demonstration of its enzymatic activity [FEBS Letters 516 (2002) 183-186], we report herein the cloning of its full-length cDNA sequence. The open reading frame encodes a protein of 511 amino acids. Results of RT-PCR indicate that antiquitin is highly expressed in both the seabream liver and kidney. Transfection studies in cultured eukaryotic cells provided further evidence that it is a cytosolic protein. Bacterial expression of the enzyme was also performed. The purified recombinant protein was demonstrated to exhibit similar kinetic properties as the native enzyme. © 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | - |
dc.language | eng | - |
dc.relation.ispartof | FEBS Letters | - |
dc.subject | Aldehyde dehydrogenase | - |
dc.subject | Antiquitin | - |
dc.subject | ALDH7A1 | - |
dc.subject | Tissue distribution | - |
dc.subject | Subcellular localization | - |
dc.subject | Eukaryotic expression | - |
dc.title | Seabream antiquitin: Molecular cloning, tissue distribution, subcellular localization and functional expression | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1016/j.febslet.2005.05.070 | - |
dc.identifier.pmid | 15967446 | - |
dc.identifier.scopus | eid_2-s2.0-21244500981 | - |
dc.identifier.volume | 579 | - |
dc.identifier.issue | 17 | - |
dc.identifier.spage | 3759 | - |
dc.identifier.epage | 3764 | - |
dc.identifier.isi | WOS:000230335600046 | - |
dc.identifier.issnl | 0014-5793 | - |