Conformational properties of disulfide-free recombinant chicken ovalbumin

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Title
Conformational properties of disulfide-free recombinant chicken ovalbumin
Author(s)
Yeon Hee Jeoung; Myeong Hee Yu
Bibliographic Citation
BMB Reports, vol. 32, no. 3, pp. 247-253
Publication Year
1999
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.
Keyword
Conformational stabilityHigh-level expressionOvalbumin
ISSN
1225-8687
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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