Applied Microbiology and Biotechnology

, Volume 49, Issue 1, pp 31–38

Purification and characterization of recombinant spider silk expressed in Escherichia coli

  • S. Arcidiacono
  • C. Mello
  • D. Kaplan
  • S. Cheley
  • H. Bayley
ORIGINAL PAPER

DOI: 10.1007/s002530051133

Cite this article as:
Arcidiacono, S., Mello, C., Kaplan, D. et al. Appl Microbiol Biotechnol (1998) 49: 31. doi:10.1007/s002530051133

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.

Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • S. Arcidiacono
    • 1
  • C. Mello
    • 1
  • D. Kaplan
    • 2
  • S. Cheley
    • 3
  • H. Bayley
    • 3
  1. 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 5521US
  2. 2.Tufts University, Medford, MA 02155, USAUS
  3. 3.Texas A&M University, College station, TX 77843, USAUS