The Role of the Disulfide Bridge in the Stability and Structural Integrity of Ovalbumin Evaluated by Site-Directed Mutagenesis
-
- ISHIMARU Takayuki
- Department of Biological Chemistry, Yamaguchi University
-
- ITO Kazunari
- Industrial Technology Center of Okayama Prefecture
-
- TANAKA Miho
- Department of Biological Chemistry, Yamaguchi University
-
- TANAKA Syunpei
- Department of Biological Chemistry, Yamaguchi University
-
- MATSUDOMI Naotoshi
- Department of Biological Chemistry, Yamaguchi University
この論文をさがす
抄録
To provide a molecular explanation of the role of the disulfide (SS) bridge in the thermostability and structural integrity of ovalbumin (OVA), we prepared SS-mutated OVAs in which SS-forming residues were replaced by Ala or Ser (C73A, C73S, C120A, and C73/120A), and compared the conformation, thermostability, susceptibility to elastase, and formation of heat-stable OVA (S-OVA) with those of the wild-type. The circular dichroism (CD) and tryptophan fluorescence spectra revealed that the SS-mutated OVAs assumed a native-like conformation similar to the wild-type. The thermal denaturation temperature for the SS-mutated OVAs was significantly lower than that for the wild-type. C73S, C120A, and C73/120A mutants converted to S-OVA on alkaline treatment. Analyses for elastase digestion fragments showed that a non-native SS bridge was generated in all SS-mutated OVAs, but non-native SS-pairing did not contribute to thermostability. Hence, we concluded that the presence of the original SS bridge in OVA contributes to conformational stability but is not directly related to the conversion to S-OVA.
収録刊行物
-
- Bioscience, Biotechnology, and Biochemistry
-
Bioscience, Biotechnology, and Biochemistry 75 (3), 544-549, 2011
公益社団法人 日本農芸化学会
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1390282681453805952
-
- NII論文ID
- 10028201913
-
- NII書誌ID
- AA10824164
-
- ISSN
- 13476947
- 09168451
-
- NDL書誌ID
- 11051749
-
- 本文言語コード
- en
-
- データソース種別
-
- JaLC
- NDL
- Crossref
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可