DPP IV has been attributed a large array of functions, some of which are mediated by its exopeptidase activity. Although it only removes two amino acid residues at the N-terminus of the peptide, this cleavage can inactivate or modify the activity of regulatory peptides, peptide hormones, chemokines and neuropeptides. Several excellent DPP IV substrates with high specificity constants were identified by the in vitro kinetic study of the truncation of bioactive peptides by DPP IV. In vivo studies . with DPP IV negative animals and in vivo inhibition experiments could enlighten us on the physiological relevance of these truncations. The DPP IV mediated truncation of bioactive peptides.
