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ID 46955
FullText URL
Author
Kanayama, Naoki ORCID Kakenhi
Yamakoshi, Kimi
Kiyomi, Masaaki
Abstract
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.
Published Date
2004-03
Publication Title
Memoirs of the Faculty of Engineering, Okayama University
Volume
volume38
Issue
issue1-2
Publisher
Faculty of Engineering, Okayama University
Start Page
91
End Page
96
ISSN
0475-0071
NCID
AA10699856
Content Type
Departmental Bulletin Paper
language
英語
File Version
publisher
Refereed
False
Eprints Journal Name
mfe