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The Isolation, Differentiation, and Quantification of Human Antibody-secreting B Cells from Blood: ELISpot as a Functional Readout of Humoral Immunity
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Purified and cell-bound CD26: enzymatic inhibition, antibody binding profile, and expression on T cells in relation

S Scharpe1, I De Meester

  • 1Laboratorium Medische Biochemie, Universitaire Instelling Antwerpen, Wilrijk.

Verhandelingen - Koninklijke Academie Voor Geneeskunde Van Belgie
|January 1, 1994
PubMed

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).

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