title: Production of a recombinant full-length prion protein in a soluble form without refolding or detergents.
abstract: 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.
authors.affiliation: Department of Food Science and Nutrition, Mukogawa Women's University, Nishinomiya, Hyogo, Japan. arii@mukogawa-u.ac.jp
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Arii
authors.forename: Satoshi
authors.initials: S
authors.lastname: Oshiro
authors.forename: Keita
authors.initials: K
authors.lastname: Wada
authors.forename: Shin-ichi
authors.initials: S
authors.lastname: Fukuoka
mesh_terms: D000818:Animals; D015153:Blotting, Western; D004926:Escherichia coli; D015870:Gene Expression; D006801:Humans; D051379:Mice; D020890:Neuregulin-1 / Q000235:genetics* / Q000378:metabolism; D010957:Plasmids; D017096:Prion Diseases / Q000378:metabolism / Q000503:physiopathology; D011328:Prions / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D017510:Protein Folding; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D012995:Solubility; D013050:Spectrometry, Fluorescence; D014169:Transformation, Bacterial
chemical_list: D020890:Neuregulin-1; D011328:Prions; D011994:Recombinant Proteins; C117467:neuregulin beta