| Title : Purified and cell-bound CD26: enzymatic inhibition, antibody binding profile, and expression on T cells in relation to other surface markers - Scharpe_1994_Verh.K.Acad.Geneeskd.Belg_56_537 |
| Author(s) : Scharpe S , De Meester I |
| Ref : Verh K Acad Geneeskd Belg , 56 :537 , 1994 |
|
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). We investigated some molecular and inhibition characteristics as well as the monoclonal antibody (mAb)-binding profile of this molecule purified from human lymphocytes. Among the antibodies we explored, two, anti-BT5/9 and anti-TA5.9, exhibited a high affinity for both purified and cell-bound CD26 Ag. Their significance in the study of immunologic memory and lymphocyte activation is discussed in relation to other markers of lymphocyte activation. Among 4 types of inhibitors studied, Pro-boroPro proved to be the most promising substance for further research on the physiological role of dipeptidyl peptidase IV (CD26). |
| PubMedSearch : Scharpe_1994_Verh.K.Acad.Geneeskd.Belg_56_537 |
| PubMedID: 7892748 |
| Inhibitor | Pro-boropro |
Scharpe S, De Meester I (1994)
Purified and cell-bound CD26: enzymatic inhibition, antibody binding profile, and expression on T cells in relation to other surface markers
Verh K Acad Geneeskd Belg
56 :537
Scharpe S, De Meester I (1994)
Verh K Acad Geneeskd Belg
56 :537