Expression in E. coli and purification of the nucleoside diphosphate kinase b from Leishmania major

Protein Expr Purif. 2006 Oct;49(2):244-50. doi: 10.1016/j.pep.2006.05.010. Epub 2006 May 26.

Abstract

Leishmaniasis is considered by the World Health Organization to be the second most important disease caused by a protozoan parasite. Biochemical and molecular biology studies can help in the understanding of the biology of the Leishmania parasite. All protozoan parasites, including Leishmania, are unable to synthesize purines de novo, and nucleoside diphosphate kinases (NDK) are involved in the salvage pathway by which free purines are converted to nucleosides and subsequently to nucleotides. In this report, we describe the cloning of NDK coding-sequence from Leishmania major, the expression of the enzyme containing a His(6)-tag in Escherichia coli, and purification of the catalytically active native protein by affinity chromatography using Ni-NTA resin.

MeSH terms

  • Animals
  • Base Sequence
  • Escherichia coli* / genetics
  • Humans
  • Leishmania major / enzymology*
  • Leishmania major / genetics
  • Leishmaniasis, Cutaneous / enzymology
  • Leishmaniasis, Cutaneous / epidemiology
  • Leishmaniasis, Cutaneous / genetics
  • Molecular Sequence Data
  • Nucleoside-Diphosphate Kinase / biosynthesis*
  • Nucleoside-Diphosphate Kinase / genetics
  • Nucleoside-Diphosphate Kinase / isolation & purification*
  • Protozoan Proteins / biosynthesis*
  • Protozoan Proteins / isolation & purification*
  • Recombinant Fusion Proteins / biosynthesis*
  • Recombinant Fusion Proteins / isolation & purification*

Substances

  • Protozoan Proteins
  • Recombinant Fusion Proteins
  • Nucleoside-Diphosphate Kinase