title: Enhancement of the activity of renatured lysozyme by protein disulfide isomerase.
abstract: The coexistence of protein disulfide isomerase (PDI) in the oxidative refolding of a fully reduced hen egg white lysozyme brought about a final recovered activity significantly exceeding 100% in addition to the expected acceleration effect. This increase could not be explained by the simple increase produced by suppressing aggregation. After examination of the starting material and assay system, it was concluded that PDI enhances the activity of renatured lysozyme.
authors.affiliation: Department of Biomolecular Science, Faculty of Engineering, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan.
authors.forename: Daisuke
authors.initials: D
authors.lastname: Nohara
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Hizikata
authors.forename: Osamu
authors.initials: O
authors.lastname: Asami
mesh_terms: D004789:Enzyme Activation; D004795:Enzyme Stability; D009113:Muramidase / Q000737:chemistry*; D011489:Protein Denaturation; D019704:Protein Disulfide-Isomerases / Q000737:chemistry*; D017510:Protein Folding
chemical_list: C421864:hen egg lysozyme; D009113:Muramidase; D019704:Protein Disulfide-Isomerases