Titlebook: Dipeptidyl Aminopeptidases; Basic Science and Cl Uwe Lendeckel,Dirk Reinhold,Ute Bank Conference proceedings 2006 The Editor(s) (if applica

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Biochemical Properties of Recombinant Prolyl Dipeptidases DPP-IV and DPP8

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In Vivo Effects of a Potent, Selective Dppii Inhibitor

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Expression of Dipeptidyl Peptidase IV-Like Enzymes in Human Peripheral Blood Mononuclear Cells

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Distribution of Dipeptidyl Peptidase Iv-Like Activity Enzymes in Canine and Porcine Tissue Sections

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Structure and Function in Dipeptidyl Peptidase IV and Related Proteinsrts are confounded by the ubiquitous expression of DPIV, inhibitor selectivity questions and the variety of identified substrates. DPIV is not essential, but is such a useful enzyme that all animal species express it. The enzyme activity’s ancient and primary function is probably nutritional, provid

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Dipeptidyl Peptidase 8 Has Post-Proline Dipeptidyl Aminopeptidase and Prolyl Endopeptidase Activitieifically has both prolyl dipeptidyl aminopeptidase and PEP activities. DPIV inhibitors varied in their selectivity against DP8 but all DP8 activities were inhibited by the irreversible DPIV inhibitor ValboroPro. These data indicate that DP8 is a multifunctional enzyme and that therapeutics based on