Refolding of urea-denatured ovalbumin that comprises non-native disulfide isomers.

Refolding of urea-denatured ovalbumin that comprises non-native disulfide isomers. Research Abstract Details 

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Refolding of urea-denatured ovalbumin that comprises non-native disulfide isomers. Abstract Text:

M Onda,E Tatsumi,N Takahashi,M Hirose,

Ovalbumin, which contains one cystine disulfide (Cys73-Cys120) and four cysteine sulfhydryls (Cys11, Cys30, Cys367, and Cys382) in the native state, undergoes intrachain sulfhydryl-disulfide exchanges at high concentrations of urea, generating many non-native disulfide isomers [E. Tatsumi, N. Takahashi, and M. Hirose (1994) J. Biol. Chem. 269, 28062-28067]. The refolding of ovalbumin from the urea-denatured state was investigated. When the denatured protein was diluted 20-fold with a refolding buffer (pH 8.2), an initial burst intermediate I(N) was produced within the 20 ms instrumental dead time; I(N) showed about 60% of the native CD ellipticity at 222 nm. The intrinsic tryptophan fluorescence of I(N) showed the same peak (338 nm), but with decreased intensity (57%), as compared to the native protein. After the rapid formation of I(N), most of the ovalbumin molecules correctly refolded into the native state with slow biphasic kinetics, as evaluated by far-UV CD, tryptophan fluorescence, and trypsin-resistance analyses. Furthermore, a peptide-mapping analysis revealed that sulfhydryl/disulfide exchange reactions occurred during the refolding, thereby increasing the formation of the native disulfide. The integrity of overall refolding was confirmed by a differential scanning calorimetry analysis. These data were consistent with the view that most, if not all, of the mispaired disulfide isomers in the urea-denatured ovalbumin can correctly refold into the native state via intrachain disulfide rearrangements.

Refolding of urea-denatured ovalbumin that comprises non-native disulfide isomers. Publishing Authors By Initials

M Onda,E Tatsumi,N Takahashi,M Hirose,

For similar organic chemicals: urea research abstracts see: organic chemicals: urea research

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Refolding of urea-denatured ovalbumin that comprises non-native disulfide isomers. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 122

Page Numbers: 83-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1997

Refolding of urea-denatured ovalbumin that comprises non-native disulfide isomers. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Refolding of urea-denatured ovalbumin that comprises non-native disulfide isomers. Keywords Mesh Terms:

KEYWORDS: Urea

MESH TERMS: chemistry

Chemical & Substance for Abstract: Refolding of urea-denatured ovalbumin that comprises non-native disulfide isomers. Information

Substance Name: Ovalbumin

Registry Number: 9006-59-1

Grant and Affiliation Information for Refolding of urea-denatured ovalbumin that comprises non-native disulfide isomers.

AFFILIATION: The Research Institute for Food Science, Kyoto University.

Country: JAPAN

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MEDLINETA: J Biochem

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