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Title 

Conformational properties of disulfide-free recombinant chicken ovalbumin

Authors 

Yeon Hee JeoungMyeong 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 stabilityHigh-level expressionOvalbumin

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

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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