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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Seabream antiquitin: molecular cloning, tissue distribution, subcellular localization and functional expression.

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.[1]

References

  1. Seabream antiquitin: molecular cloning, tissue distribution, subcellular localization and functional expression. Tang, W.K., Chan, C.B., Cheng, C.H., Fong, W.P. FEBS Lett. (2005) [Pubmed]
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