Abstract
The plasmid DNA pERilox4 containing the gene of the recombinant protein, which included the leader sequence and the oxytocinoyl lysine tetramer, was constructed. The high level of gene expression in E. coli was achieved. The method for purification of the recombinant protein and its isolation in the soluble form was developed. The conditions for digestion of the hybrid protein by trypsin and carboxypeptidase B were matched. The effective method for transformation of oxytocinic acid to oxytocin was worked out. The scheme suggested allowed obtaining oxytocin in high yield.
Keywords: oxytocin, hybrid protein enzymatic cleavage, c-terminal amide
Protein & Peptide Letters
Title: Production And Purification Of Recombinant Human Oxytocin Overexpressed As A Hybrid Protein In Escherichia Coli
Volume: 10 Issue: 4
Author(s): Roman S. Esipov, Larisa A. Chupova, Sergey V. Shvets, Dmitry V. Chuvikovsky, Alexandr I. Gurevich, Tatyana I. Muravyova and Anatoly I. Miroshnikov
Affiliation:
Keywords: oxytocin, hybrid protein enzymatic cleavage, c-terminal amide
Abstract: The plasmid DNA pERilox4 containing the gene of the recombinant protein, which included the leader sequence and the oxytocinoyl lysine tetramer, was constructed. The high level of gene expression in E. coli was achieved. The method for purification of the recombinant protein and its isolation in the soluble form was developed. The conditions for digestion of the hybrid protein by trypsin and carboxypeptidase B were matched. The effective method for transformation of oxytocinic acid to oxytocin was worked out. The scheme suggested allowed obtaining oxytocin in high yield.
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Cite this article as:
Esipov S. Roman, Chupova A. Larisa, Shvets V. Sergey, Chuvikovsky V. Dmitry, Gurevich I. Alexandr, Muravyova I. Tatyana and Miroshnikov I. Anatoly, Production And Purification Of Recombinant Human Oxytocin Overexpressed As A Hybrid Protein In Escherichia Coli, Protein & Peptide Letters 2003; 10 (4) . https://dx.doi.org/10.2174/0929866033478807
DOI https://dx.doi.org/10.2174/0929866033478807 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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