Purification and characterization of recombinant spider silk expressed in Escherichia coli

@article{Arcidiacono1998PurificationAC,
  title={Purification and characterization of recombinant spider silk expressed in Escherichia coli},
  author={S. Arcidiacono and C. Mello and D. Kaplan and S. Cheley and H. Bayley},
  journal={Applied Microbiology and Biotechnology},
  year={1998},
  volume={49},
  pages={31-38}
}
  • S. Arcidiacono, C. Mello, +2 authors H. Bayley
  • Published 1998
  • Biology, Medicine
  • Applied Microbiology and Biotechnology
    • Abstract A partial cDNA clone, from the 3′ end of the dragline silk gene was isolated from Nephila clavipes major ampullate glands. This clone contains a 1.7-kb insert, consisting of a repetitive coding region of 1.4-kb and a 0.3-kb nonrepetitive coding region; 1.5-kb of the 1.7-kb fragment was cloned into Escherichia coli and a␣43-kDa recombinant silk protein was expressed. Characterization of the purified protein by Western blot, amino acid composition analysis, and matrix-assisted laser… CONTINUE READING
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