Purification and On-Column Activation of a Recombinant Histidine-Tagged Pro-Transglutaminase after Soluble Expression in Escherichia coli

Hui-Lin YANG; Li PAN; Ying LIN

doi:10.1271/bbb.90422

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Purification and On-Column Activation of a Recombinant Histidine-Tagged Pro-Transglutaminase after Soluble Expression in Escherichia coli

Hui-Lin YANG, Li PAN, Ying LIN

著者情報

キーワード: microbial transglutaminase, soluble recombinant expression, high-density culture, Escherichia coli, on-column activation

ジャーナルフリー早期公開

論文ID: 90422

DOI https://doi.org/10.1271/bbb.90422

この記事には本公開記事があります。

The final version of this article is now available: Vol. 73 (2009) , No. 11 p.2531

詳細

抄録

Microbial transglutaminase (MTG) is widely used as a protein crosslinking enzyme. Pro-transglutaminase from Streptomyces mobaraensis was expressed in Escherichia coli as a fusion protein carrying a C-terminal histidine tag (pro-MTG-His₆) under high-density culture. A new method of on-column activation was designed for production. According to SDS–PAGE, 88.9% of pro-MTG-His₆ was transferred to mature MTG-His₆ with storage stabilization.

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