Protein Refolding in Nanostructured Reversed Micelles Including a Molecular Chaperone(BIOCHEMICAL ENGINEERING)
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概要
- 論文の詳細を見る
Reversed micelles including the molecular chaperone GroEL were applied to the protein refolding of denatured RNase A. The molecular chaperone was successfully functionalized in the water pools of the reversed micelles sharing a structural size of 15-25 nm. The refolding yield of RNase A in the reversed-micelle/GroEL system was much greater than that of spontaneous renaturation. The refolding yield mediated by GroEL in the reversed micelles was strongly dependent on the presence of ATP or Mg^<2+>, suggesting that the GroEL hosted in the reversed micelles was biologically active in the micelles. Under the optimum conditions, this novel refolding technique could completely renature the denatured RNase A in 1h.
- 社団法人日本生物工学会の論文
- 2003-09-25
著者
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GOTO Masahiro
Department of Applied Chemistry, Graduate School of Engineering, Kyushu University
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Goto Masahiro
Department Of Applied Chemistry Graduate School Of Engineering Kyushu University
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Sakano Masafumi
Department Of Applied Chemstry Graduate School Of Engineering Kyushu University Hakozaki
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ICHINOSE HIROFUMI
PRESTO,JST
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Ichinose Hirofumi
Faculty Of Agriculture Kyushu University
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Goto Masahiro
Department Of Applied Biological Chemistry The University Of Tokyo
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Goto Masahiro
Department Of Applied Chemstry Graduate School Of Engineering Kyushu University Hakozaki:presto Jst
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Sakono Masafumi
Department of Applied Chemstry, Graduate School of Engineering, Kyushu University Hakozaki
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