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KMID : 0380219990320030247
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Journal of Biochemistry and Molecular Biology
1999 Volume.32 No. 3 p.247 ~ p.253
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Conformational Properties of Disulfide-Free Recombinant Chicken Ovalbumin
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Jeoung Yeon-Hee
Yu Myeong-Hee
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Abstract
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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℃. 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.
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KEYWORD
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Conformational stability, High-level expression, Ovalbumin
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