この論文をさがす
抄録
Molecular stability of chicken egg yolk immunoglobulin G (IgY) and that of rabbit IgG were compared by measuring antibody activities and conformational changes. Stability of rabbit IgG to acid denaturation was much higher than that of IgY. Conformation of the IgY molecule was readily changed in acidic conditions, resulting in a rapid loss of antibody activity. Much less stable natures of IgY to heat-treatment and guanidine-HCl denaturation than rabbit IgG were also observed. Differences in the structure between the two immunoglobulins that might participate in their different stability were inferred from their amino acid sequence data. Importance of the intramoleular disulfide linkage in the rabbit light chain and some other structural differences were suggested.
収録刊行物
-
- Bioscience, Biotechnology, and Biochemistry
-
Bioscience, Biotechnology, and Biochemistry 56 (2), 270-274, 1992
公益社団法人 日本農芸化学会
- Tweet
キーワード
詳細情報 詳細情報について
-
- CRID
- 1390001206471551360
-
- NII論文ID
- 110002680503
-
- NII書誌ID
- AA10824164
-
- COI
- 1:CAS:528:DyaK38XhslWqs7k%3D
-
- ISSN
- 13476947
- 09168451
- http://id.crossref.org/issn/09168451
-
- PubMed
- 1368302
-
- 本文言語コード
- en
-
- データソース種別
-
- JaLC
- Crossref
- PubMed
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可