Production and purification of recombinant human glucagon overexpressed as intein fusion protein in Escherichia coli

Protein Pept Lett. 2006;13(4):343-7. doi: 10.2174/092986606775974320.

Abstract

Chemico-enzymatic synthesis and cloning in Esherichia coli of an artificial gene coding human glucagon was performed. Recombinant plasmid containing hybrid glucagons gene and intein Ssp dnaB from Synechocestis sp. was designed. Expression of the obtained hybrid gene in E. coli, properties of the formed hybrid protein, and conditions of its autocatalytic cleavage leading to glucagon formation were studied.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Electrophoresis
  • Escherichia coli / metabolism
  • Glucagon / biosynthesis*
  • Humans
  • Inteins / genetics
  • Molecular Sequence Data
  • Recombinant Fusion Proteins / biosynthesis*
  • Recombinant Fusion Proteins / isolation & purification

Substances

  • Recombinant Fusion Proteins
  • Glucagon