کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
3030214 | 1183183 | 2006 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Novel monoclonal antibody that recognizes new neoantigenic determinant of D-dimer Novel monoclonal antibody that recognizes new neoantigenic determinant of D-dimer](/preview/png/3030214.png)
Our novel monoclonal antibody (mAb) B4 reacted with only D-dimer but not intact fibrinogen, or fibrinogen degradation products (FgDP) such as D-monomer, E fragment on ELISA. B4 didn't react with denatured D-dimer, while it reacted well with denatured D-monomer rather than the native form, indicating that B4 recognizes some neoconformational epitope in D-dimer. In our epitope study, B4 recognized the N-terminal (Bβ134-142) of D-dimer, which corresponds to the most flexible segment of coiled coil backbone. It was confirmed by inhibition assay of B4 binding to D-dimer using the synthesized peptides with this sequence. As the other evidence, B4 didn't bind to some D-dimer species produced from a particular fibrinogen variant. This fibrinogen variant is mutated BβLys133 residue to Gln133 thus it doesn't produce the particular N-terminal epitope of D134∼ by plasmin. Finally, our mAb was useful for clinical application. ELISA using our mAbs was well correlated with other commercial D-dimer ELISAs and in some clinical samples it was preferable to them. These results suggest that the epitope for B4 is another neoantigenic determinant in native D-dimer as distinct from native D-monomer.
Journal: Thrombosis Research - Volume 118, Issue 3, 2006, Pages 353–360