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. 2003 Aug;10(4):404-11.
doi: 10.2174/0929866033478807.

Production and purification of recombinant human oxytocin overexpressed as a hybrid protein in Escherichia coli

Roman S Esipov  1 , Larisa A Chupova, Sergey V Shvets, Dmitry V Chuvikovsky, Alexandr I Gurevich, Tatyana I Muravyova, Anatoly I Miroshnikov
Affiliations

Production and purification of recombinant human oxytocin overexpressed as a hybrid protein in Escherichia coli

Roman S Esipov et al. Protein Pept Lett. 2003 Aug.

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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