| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2014-01-15 |
| タイトル |
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タイトル |
Kinetics of disulfide bond reduction in .alpha.-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond |
| タイトル |
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タイトル |
Kinetics of disulfide bond reduction in .alpha.-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond |
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言語 |
en |
| 言語 |
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言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| アクセス権 |
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アクセス権 |
metadata only access |
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アクセス権URI |
http://purl.org/coar/access_right/c_14cb |
| 著者 |
KUWAJIMA, Kunihiro
IKEGUCHI, Masamichi
SUGAWARA, Tatsuro
HIRAOKA, Yoshiki
SUGAI, Shintaro
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| 著者別名 |
桑島, 邦博
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| 抄録 |
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内容記述タイプ |
Abstract |
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内容記述 |
The reversible equilibrium unfolding of carp parvalbumin III (pI = 4.25) when treated with guanidine hydrochloride and the kinetics of folding and unfolding induced by concentration jump of the denaturant have been studied by the peptide circular dichroism spectra at pH 7.0 and 4.5°C. In the kinetic refolding reaction, a transient folding intermediate was found to be rapidly accumulated within the dead time of the stopped-flow circular dichroism (18 ms). The preequilibrium unfolding curve corresponding to the unfolding curve of the transient intermediate was obtained by measuring the refolding kinetics at various concentrations of the denaturant. Comparison of the equilibrium and preequilibrium unfolding curves has demonstrated that the total equilibrium reaction is well interpreted in terms of a three-state mechanism in which the intermediate, identical with the transient intermediate, is populated at low concentrations of the denaturant. The intermediate has been shown to have the following properties: (i) It has 60-80% of the α-helix in the native protein but does not have the specific structure responsible for strong Ca2+ binding; (ii) it is similar to the partially unfolded state observed at acid pH. Effects of Ca2+ on the unfolding equilibrium and on the refolding kinetics have also been investigated. The results have demonstrated the stepwise organization of the substructures of parvalbumin during its refolding. As a conclusion, the folding process of this protein can be divided into the three stages: (i) rapid formation of the secondary structure framework; (ii) organization of a part of the specific tertiary structure including one of the two Ca2+-binding domains, with this step leading to the activated state of folding; and (iii) the final stabilization associated with organization of the rest of the molecule including the other Ca2+-binding domain. |
| 書誌情報 |
Biochemistry
en : Biochemistry
巻 29,
号 36,
p. 8240-8249,
発行日 1990-09
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| 出版者 |
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出版者 |
American Chemical Society |
| ISSN |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
00062960 |
| DOI |
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識別子タイプ |
DOI |
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関連識別子 |
http://doi.org/10.1021/bi00488a007 |
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関連名称 |
10.1021/bi00488a007 |
| 権利 |
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権利情報 |
© 1990 American Chemical Society |
