このエントリーをはてなブックマークに追加
ID 46955
フルテキストURL
著者
Kanayama, Naoki Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University ORCID Kaken ID
Yamakoshi, Kimi Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University
Kiyomi, Masaaki Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University
Magari, Masaki Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University
Ohmori, Hitoshi Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University
抄録
Generally, IgM antibodies (Abs) produced in a primary immune response show lower affinity for an inducing antigen (Ag) compared with the corresponding IgG Abs that are major switched isotypes formed in the secondary response. An IgM molecule is a pentamer with 10 Ag-binding sites that will contribute to an increase of avidity for an Ag. To estimate the contribution of the pentameric structure to the avidity of an IgM Ab, we generated IgM and IgG1 monoclonal Abs (mAbs) with identical V regions that are specific for 4-hydroxy-3-nitrophenylacetyl (NP) by in vitro class switching of B cells followed by the cell fusion with a mouse myeloma cell line. Compared with an anti-NP IgG1 mAb, the corresponding IgM mAb showed much higher avidity for NP-conjugated bovine serum albumin, which was drastically reduced after being dissociated into monomers.
発行日
2004-03
出版物タイトル
Memoirs of the Faculty of Engineering, Okayama University
38巻
1-2号
出版者
Faculty of Engineering, Okayama University
開始ページ
91
終了ページ
96
ISSN
0475-0071
NCID
AA10699856
資料タイプ
紀要論文
言語
English
論文のバージョン
publisher
査読
無し
Eprints Journal Name
mfe