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MethodsX. 2021 Sep 16;8:101517. doi: 10.1016/j.mex.2021.101517. eCollection 2021.

Optimization of production of recombinant gamma-tubulin in bacteria.

MethodsX

Jingkai Zhou, Maria Alvarado-Kristensson

Affiliations

  1. Molecular Pathology, Department of Translational Medicine, Lund University, Jan Waldenströms gata 59, Malmö SE-205 02, Sweden.

PMID: 34754788 PMCID: PMC8563660 DOI: 10.1016/j.mex.2021.101517

Abstract

Production of a protein of interest in bacteria and its purification from bacterial lysates are valuable tools for the purification of larger amounts of recombinant proteins. The low cost of culturing, and the rapid cell growth of bacteria make this host a good choice for protein production, but the folding and function of the purified protein might be altered due to the production of a eukaryotic protein in a prokaryotic host. Here, we provide a purification method for the purification of gamma (γ)-tubulin (TUBG) from soluble fractions of

© 2021 The Authors. Published by Elsevier B.V.

Keywords: Bacteria; Gamma-tubulin; Native protein; Protein purification; Recombinant protein

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