Purification and characterization of recombinant spider silk expressed in Escherichia coli

Appl Microbiol Biotechnol. 1998 Jan;49(1):31-8. doi: 10.1007/s002530051133.


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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • DNA, Complementary / chemistry
  • Escherichia coli / genetics*
  • Insect Proteins / biosynthesis*
  • Insect Proteins / chemistry
  • Insect Proteins / isolation & purification
  • Molecular Sequence Data
  • Recombinant Proteins / biosynthesis*
  • Recombinant Proteins / isolation & purification
  • Silk
  • Spiders


  • DNA, Complementary
  • Insect Proteins
  • Recombinant Proteins
  • Silk

Associated data

  • GENBANK/U20329