Renaturation of lysozyme with a protein disulfide isomerase chaperone results in enzyme super activity.
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.
Takezawa
Aya
A
Department of Biomolecular Science, Faculty of Engineering, Gifu University, 1-1 Yanagido, Gifu, Japan.
Ohshima
Yuji
Y
Sudo
Tomoya
T
Asami
Osamu
O
Nohara
Daisuke
D
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
D004220:Disulfides; D018832:Molecular Chaperones; D009113:Muramidase; D019704:Protein Disulfide-Isomerases; D010100:Oxygen