Production of a Recombinant Full-Length Prion Protein in a Soluble Form without Refolding or Detergents
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概要
- 論文の詳細を見る
Recombinant prion protein has been produced in insoluble form and refolded following solubilization with denaturants. It is, however, preferable to use a soluble recombinant protein prepared without artificial solubilization. In this study, a soluble recombinant prion protein was produced in Escherichia coli cells by coexpression of neuregulin I-β1 and purified to high purity.
- 社団法人 日本農芸化学会の論文
著者
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Fukuoka Shin-Ichi
Biological Science Course, Graduate School of Science and Engineering, Aoyama Gakuin University
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ARII YASUHIRO
Department of Chemistry, School of Science and Engineering, Kinki University
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Arii Yasuhiro
Department Of Chemistry School Of Science And Engineering Kinki University
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Arii Yasuhiro
Laboratory Of Molecular Cell Biology Department Of Chemistry And Biological Science College Of Scien
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OSHIRO Satoshi
Biological Science Course, Graduate School of Science and Engineering, Aoyama Gakuin University
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WADA Keita
Biological Science Course, Graduate School of Science and Engineering, Aoyama Gakuin University
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Fukuoka Shin-ichi
Biological Sci. Course Graduate School Of Sci. And Engineering Aoyama Gakuin Univ.
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