[Human erythrocyte prolyl endopeptidase II hydrolysing teprotid, an inhibitor of peptidyl peptidase from snake venom].

The paper is concerned with the action of 1200-fold purified prolylendopeptidase II (PE-E) from human erythrocytes and the action of highly purified prolyl-D-L-alanine peptidyl hydrolase (PE-A) from bovine adenohypophysis on teprotide (BPP9a, SQ 20881), a nonapeptide from venom of the snake Bothrops Jararaca--an inhibitor of peptidyl dipeptidase A (carboxycathepsin). Both the purified preparation PE-E and highly purified preparation PE-A split teprotide at the bonds Pro3-Arg4 and Pro5-Gln6. The Pro8-Pro9-OH bond was not split by the two enzymes. The comparative characteristics of the properties of PE-E and PE-A are presented and the possible physiological role of these enzymes is discussed.