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Purification and characterization of recombinant spider silk expressed in Escherichia coli

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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 desorption ionization/time-of-flight mass spectrometry confirms it to be spider dragline silk.

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Authors and Affiliations

  1. Biotechnology Division, U.S. Army Natick Army Research, Development, and Engineering Center, Natick, MA 01760, USA Tel.: +1 (508) 233 5513; Fax: +1 (508) 233 5521, , , , , , US

    S. Arcidiacono & C. Mello

  2. Tufts University, Medford, MA 02155, USA, , , , , , US

    D. Kaplan

  3. Texas A&M University, College station, TX 77843, USA, , , , , , US

    S. Cheley & H. Bayley

Authors
  1. S. Arcidiacono
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  2. C. Mello
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  3. D. Kaplan
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  4. S. Cheley
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  5. H. Bayley
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Additional information

Received: 7 April 1997 / Received revision: 24 July 1997 / Accepted: 25 August 1997

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Arcidiacono, S., Mello, C., Kaplan, D. et al. Purification and characterization of recombinant spider silk expressed in Escherichia coli . Appl Microbiol Biotechnol 49, 31–38 (1998). https://doi.org/10.1007/s002530051133

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  • DOI: https://doi.org/10.1007/s002530051133

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