Abstract
The CD26 activation antigen (Ag) which is expressed on a subpopulation of human T cells has been characterized as dipeptidyl peptidase IV (DPP IV, EC 3.4.14.5).In this paper, we describe the antibody binding profile of CD26/DPP IV, purified from human peripheral blood lymphocytes.The purified molecule binds to the anti-Ta1, anti-1F7 and anti-134-2C2 monoclonal antibodies (mAb), reported to react with cell-bound CD26 Ag.Among unclustered mAb recognizing T cell antigens, two, anti-BT5/9 and anti-TA5.9 were found to react with purified and cell-bound CD26 Ag.The classification of the BT5/9 Ag, the functional properties of the BT5/9+ T cell subset, as well as the in vivo effect of anti-BT5/9 mAb administration, are re-interpreted in the light of its specificity.
Applying the anti-TA5.9 mAb in three color FACS analyses, we demonstrated that CD26+bright cells co-express CD45RO but not HLA-DR and CD38.
Applying the anti-TA5.9 mAb in three color FACS analyses, we demonstrated that CD26+bright cells co-express CD45RO but not HLA-DR and CD38.
| Original language | English |
|---|---|
| Journal | Immunobiology |
| Volume | 188 |
| Issue number | 1-2 |
| Pages (from-to) | 145-158 |
| Number of pages | 8 |
| DOIs | |
| Publication status | Published - 1993 |
Keywords
- B780-tropical-medicine
- Virology
- Immunology
- Experimental
- CD26