Production And Purification Of Recombinant Human Oxytocin Overexpressed As A Hybrid Protein In Escherichia Coli

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.

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