| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 21529 | Journal of Bioscience and Bioengineering | 2008 | 4 Pages |
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.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Aya Takezawa, Yuji Ohshima, Tomoya Sudo, Osamu Asami, Daisuke Nohara,