or
Title | Conformational properties of disulfide-free recombinant chicken ovalbumin |
Authors | Yeon Hee Jeoung; Myeong Hee Yu |
Publisher | Springer Verlag (Germany) |
Issue Date | 1999 |
Citation | Journal of Biochemistry and Molecular Biology, vol. 32, no. 3, pp. 247-253 |
Keywords | Conformational stability; High-level expression; Ovalbumin |
Abstract | Chicken egg ovalbumin is a non-inhibitory member of the serpin (serine protease inhibitors) family whose members share a common tertiary fold. In the present study, we succeeded in high-level production of a disulfide-free form of refolded recombinant ovalbumin. Conformational characterization of the recombinant ovalbumim revealed that it is well-folded, following two-state unfolding transition with the midpoint of transition at 4.7 M at 25°C. This value is very close to that of the reduced form of authentic ovalbumin. The recombinant ovalbumin can serve as a model molecule of non-inhibitory serpins in comparative studies with inhibitory members of the serpin family. |
ISSN | 1225-8687 |
Appears in Collections | |
Registered Date |
2017-04-19 |
