Conformational properties of disulfide-free recombinant chicken ovalbumin

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dc.contributor.authorYeon Hee Jeoung-
dc.contributor.authorMyeong Hee Yu-
dc.date.accessioned2017-04-19T08:56:01Z-
dc.date.available2017-04-19T08:56:01Z-
dc.date.issued1999-
dc.identifier.issn1225-8687-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4698-
dc.description.abstractChicken 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.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleConformational properties of disulfide-free recombinant chicken ovalbumin-
dc.title.alternativeConformational properties of disulfide-free recombinant chicken ovalbumin-
dc.typeArticle-
dc.citation.titleBMB Reports-
dc.citation.number3-
dc.citation.endPage253-
dc.citation.startPage247-
dc.citation.volume32-
dc.contributor.affiliatedAuthorYeon Hee Jeoung-
dc.contributor.affiliatedAuthorMyeong Hee Yu-
dc.contributor.alternativeName정연희-
dc.contributor.alternativeName유명희-
dc.identifier.bibliographicCitationBMB Reports, vol. 32, no. 3, pp. 247-253-
dc.subject.keywordConformational stability-
dc.subject.keywordHigh-level expression-
dc.subject.keywordOvalbumin-
dc.subject.localConformational stability-
dc.subject.localHigh-level expression-
dc.subject.localhigh-level expression-
dc.subject.localOvalbumin-
dc.subject.localOvalbumin (OVA)-
dc.subject.localovalbumin-
dc.description.journalClassY-
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