Isolation and characterization of a mouse amelogenin expressed in Escherichia coli

@article{Simmer1994IsolationAC,
  title={Isolation and characterization of a mouse amelogenin expressed in Escherichia coli},
  author={James P. Simmer and Eduardo C. Lau and C. C. Hu and Takaaki Aoba and M. F. Lacey and David Nelson and Margarita Zeichner-David and Malcolm L Snead and Harold C. Slavkin and Alan G. Fincham},
  journal={Calcified Tissue International},
  year={1994},
  volume={54},
  pages={312-319}
}
A mouse cDNA encoding a 180 amino acid amelogenin was subcloned into the pET expression plasmid (Novagen, Madison, WI) for production in Escherichia coli. A simple growth and purification protocol yields 20–50 mg of 95–99% pure recombinant amelogenin from a 4.5-liter culture. This is the first heterologous expression of an enamel protein. The expressed protein was characterized by partial Edman sequencing, amino acid composition analysis, SDS-PAGE, Western blotting, laser desorption mass… CONTINUE READING
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Amelogenin biochemistry--form and function. In: Slavkin HC, Price P (eds) Chemistry and biology of mineralized tissues

  • AG Fincham, EC Lau, JP Simmer, M Zeichner-David
  • 1992

Amelogenin biochemistryand function

  • AG Fincham, EC Lau, JP Simmer, M Zeichner-David
  • 1992

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