title: Renaturation of lysozyme with a protein disulfide isomerase chaperone results in enzyme super activity.
abstract: When the oxidative refolding of lysozyme (Lyzm) was carried out in the presence of protein disulfide isomerase (PDI) an increased refolding rate and a recovered activity exceeding 100% were reproducibly observed. The origin of this excess activity was investigated by HPLC, SDS-PAGE, and mass spectrometry and assessed using an assay for Lyzm activity. The refolding of Lyzm was achieved through the formation of PDI-Lyzm intermediates and the excess activity was derived from the nascent lysozyme released from these complexes. The released lysozyme exhibited a higher molecular activity than observed for the native protein.
authors.affiliation: Department of Biomolecular Science, Faculty of Engineering, Gifu University, 1-1 Yanagido, Gifu, Japan.
authors.forename: Aya
authors.initials: A
authors.lastname: Takezawa
authors.forename: Yuji
authors.initials: Y
authors.lastname: Ohshima
authors.forename: Tomoya
authors.initials: T
authors.lastname: Sudo
authors.forename: Osamu
authors.initials: O
authors.lastname: Asami
authors.forename: Daisuke
authors.initials: D
authors.lastname: Nohara
mesh_terms: D001709:Biotechnology / Q000379:methods*; D002851:Chromatography, High Pressure Liquid; D019281:Dimerization; D004220:Disulfides / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods; D008837:Micrococcus / Q000378:metabolism; D008956:Models, Chemical; D018832:Molecular Chaperones / Q000378:metabolism*; D009113:Muramidase / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry; D011489:Protein Denaturation; D019704:Protein Disulfide-Isomerases; D017510:Protein Folding
chemical_list: D004220:Disulfides; D018832:Molecular Chaperones; D009113:Muramidase; D019704:Protein Disulfide-Isomerases; D010100:Oxygen