Expression and Purification of Recombinant Mouse Interleukin-4 and -6 from Transgenic Rice Seeds

Molecular Biotechnology
Yoshihiro FujiwaraKenji Sekikawa

Abstract

Transgenic rice seed can be utilized as a bioreactor to produce high-value recombinant proteins. Mouse interleukin 4 (mIL-4) and mIL-6 were specifically expressed as secretory proteins in rice endosperm by ligating the N-terminal glutelin B-1 (GluB-1) signal peptide and the C-terminal KDEL endoplasmic reticulum retention signal under control of the endosperm-specific GluB-1 promoter. In the transgenic rice seed, mIL-4 and mIL-6 accumulated in levels up to 0.43 mg/g grain and 0.16 mg/g grain, respectively. The reducing agents and detergents required for extraction from the transgenic rice seeds differed between the two proteins, indicating differences in their intracellular localization within the endosperm cell. Purified mIL-4 and mIL-6 exhibited high activity and very low endotoxin contamination.

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Feb 18, 2010·Protein Expression and Purification·Yoshihiro FujiwaraKenji Sekikawa
Nov 2, 2011·Proceedings of the National Academy of Sciences of the United States of America·Yang HeDaichang Yang
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Jun 24, 2015·Plant Biotechnology Journal·Fumio TakaiwaTakachika Hiroi

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Citations

Sep 2, 2016·Plant Cell Reports·Fumio TakaiwaKenjiro Ozawa

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