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.
Keywords: Glucagon, mini-intein, autocatalitic cleavage, recombinant, polypeptide
Protein & Peptide Letters
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.
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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
DOI https://dx.doi.org/10.2174/092986606775974320 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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