Seabream antiquitin: molecular cloning, tissue ...
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Citation
| Title | Seabream antiquitin: molecular cloning, tissue distribution, subcellular localization and functional expression |
| Author(s) | W. Tang, C. Chan, C. Cheng, W. 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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