Production and Purification of Recombinant Human Glucagon Overexpressed as Intein Fusion Protein in Escherichia coli

Title: Production and Purification of Recombinant Human Glucagon Overexpressed as Intein Fusion Protein in Escherichia coli

Volume: 13 Issue: 4

Author(s): Roman S. Esipov, Vasily N. Stepanenko, Alexandr I. Gurevich, Larisa A. Chupova and Anatoly I. Miroshnikov

Affiliation:

Keywords: Glucagon, mini-intein, autocatalitic cleavage, recombinant, polypeptide

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.

Cite this article as:

Esipov S. Roman, Stepanenko N. Vasily, Gurevich I. Alexandr, Chupova A. Larisa and Miroshnikov I. Anatoly, Production and Purification of Recombinant Human Glucagon Overexpressed as Intein Fusion Protein in Escherichia coli, Protein & Peptide Letters 2006; 13 (4) . https://dx.doi.org/10.2174/092986606775974320