Purification and biochemical characterization of SELB, a translation factor involved in selenoprotein synthesis.

@article{Forchhammer1990PurificationAB,
  title={Purification and biochemical characterization of SELB, a translation factor involved in selenoprotein synthesis.},
  author={Karl Forchhammer and Karl Peter Ruecknagel and August Boeck},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 16},
  pages={9346-50}
}
The product of the selB gene from Escherichia coli is required for co-translational insertion of selenocysteine into protein. To make the SELB protein accessible to biochemical analysis, the protein was purified from cells that overexpressed the selB gene from a phage T7 promoter plasmid. It was calculated that the overproduced SELB protein was purified 20-fold. The N-terminal amino acid sequence of the purified protein was determined, and it confirmed that the initiation codon of selB mRNA… CONTINUE READING

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