期刊
PROTEIN ENGINEERING DESIGN & SELECTION
卷 31, 期 7-8, 页码 243-247出版社
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzy008
关键词
antibody-antigen interaction; disulfide bond; kappa chain; rabbit immunoglobulin G; thermal stability
资金
- JSPS KAKENHI [JP25249115, JP16H02420]
- University of Tokyo
Rabbit antibodies show unique structural characteristics in that kappa chains have an inter-domain disulfide bond between the variable and constant domains. Here we characterized this disulfide bond from physicochemical viewpoints both in stability and affinity. It was revealed that the disulfide bond contributed to the thermal stability of the antibody, but the affinity and mechanism of antigen recognition was not altered by the mutation. The present result expands the understanding of how rabbit antibodies with kappa light chains gain affinity under characteristic mechanism to gain thermal stability, and would give suggestions for the methods to artificially stabilize antibody molecules.
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