Seabream antiquitin

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Citation

Title Seabream antiquitin: molecular cloning, tissue distribution, subcellular localization and functional expression
Author(s) W. K. Tang, Catherine B. Chan, C. H. Cheng, W. P. Fong
Journal FEBS Letters
Date 2005
Volume 579
Issue 17
Start page 3759
End page 3764
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.
DOI 10.1016/j.febslet.2005.05.070

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