Expression in Escherichia coli and purification of hexahistidine-tagged human tissue transglutaminase

Protein Expr Purif. 2002 Apr;24(3):366-73. doi: 10.1006/prep.2001.1587.

Abstract

Recent evidence suggests that aberrant transglutaminase activity is associated with a wide variety of diseases. Tissue transglutaminase is the most widely distributed of the six well-characterized transglutaminases in humans. We describe a method for expressing hexahistidine-tagged human tissue transglutaminase in Escherichia coli BL21(DE3) using the pET-30 Ek/LIC expression vector. Purification of the expressed enzyme from suspensions of E. coli cells treated with CelLytic B Bacterial Cell Lysis/Extraction Reagent was accomplished by immobilized metal (Ni2+) affinity column chromatography. The procedure typically yields highly purified and highly active recombinant human tissue transglutaminase in about 1 day (about 0.6 mg/from a 1-liter culture).

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Enzyme Stability
  • Escherichia coli
  • Histidine / chemistry
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Transglutaminases / chemistry
  • Transglutaminases / genetics*
  • Transglutaminases / isolation & purification*

Substances

  • Recombinant Proteins
  • Histidine
  • Transglutaminases