Skip to main content
Log in

Purification and characterization of recombinant spider silk expressed in Escherichia coli

  • ORIGINAL PAPER
  • Published:
Applied Microbiology and Biotechnology Aims and scope Submit manuscript

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Subscribe and save

Springer+ Basic
EUR 32.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or Ebook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Author information

Authors and Affiliations

Authors

Additional information

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

Rights and permissions

Reprints and permissions

About this article

Cite this article

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

Download citation

  • Issue Date:

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

Keywords

Navigation