| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10763791 | Biochemical and Biophysical Research Communications | 2011 | 7 Pages |
Abstract
⺠HBsAg particles undergo subtle structural changes for epitope evolution via disulfide formation/isomerization. ⺠Surface plasmon resonance measurement enabled real time monitoring of antigenicity development. ⺠A neutralizing monoclonal antibody functions as a sensitive structural/functional probe. ⺠Epitope evolution of HBsAg seems to be free radical mediated and can be facilitated by redox buffer.
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Authors
Qinjian Zhao, Yang Wang, Dicky Abraham, Victoria Towne, Ronald Kennedy, Robert D. Sitrin,