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Article: Seabream antiquitin: Molecular cloning, tissue distribution, subcellular localization and functional expression

TitleSeabream antiquitin: Molecular cloning, tissue distribution, subcellular localization and functional expression
Authors
KeywordsAldehyde dehydrogenase
Antiquitin
ALDH7A1
Tissue distribution
Subcellular localization
Eukaryotic expression
Issue Date2005
Citation
FEBS Letters, 2005, v. 579, n. 17, p. 3759-3764 How to Cite?
AbstractSubsequent 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 Identifierhttp://hdl.handle.net/10722/225024
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026

 

DC FieldValueLanguage
dc.contributor.authorTang, Wai Kwan-
dc.contributor.authorChan, Chi Bun-
dc.contributor.authorCheng, Christopher H K-
dc.contributor.authorFong, Wing Ping-
dc.date.accessioned2016-04-18T11:16:32Z-
dc.date.available2016-04-18T11:16:32Z-
dc.date.issued2005-
dc.identifier.citationFEBS Letters, 2005, v. 579, n. 17, p. 3759-3764-
dc.identifier.issn0014-5793-
dc.identifier.urihttp://hdl.handle.net/10722/225024-
dc.description.abstractSubsequent 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.languageeng-
dc.relation.ispartofFEBS Letters-
dc.subjectAldehyde dehydrogenase-
dc.subjectAntiquitin-
dc.subjectALDH7A1-
dc.subjectTissue distribution-
dc.subjectSubcellular localization-
dc.subjectEukaryotic expression-
dc.titleSeabream antiquitin: Molecular cloning, tissue distribution, subcellular localization and functional expression-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.febslet.2005.05.070-
dc.identifier.pmid15967446-
dc.identifier.scopuseid_2-s2.0-21244500981-
dc.identifier.volume579-
dc.identifier.issue17-
dc.identifier.spage3759-
dc.identifier.epage3764-

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