title: [Human erythrocyte prolyl endopeptidase II hydrolysing teprotid, an inhibitor of peptidyl peptidase from snake venom].
abstract: 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.
authors.forename: L P
authors.initials: LP
authors.lastname: Alekseenko
authors.forename: V N
authors.initials: VN
authors.lastname: Orekhovich
mesh_terms: D000818:Animals; D002417:Cattle; D010450:Endopeptidases / Q000378:metabolism*; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D066298:In Vitro Techniques; D009842:Oligopeptides / Q000378:metabolism*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D010903:Pituitary Gland, Anterior / Q000201:enzymology; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases; D012910:Snake Venoms; D013722:Teprotide / Q000378:metabolism* / Q000494:pharmacology
chemical_list: D009842:Oligopeptides; D012910:Snake Venoms; D013722:Teprotide; D010450:Endopeptidases; D007703:Peptidyl-Dipeptidase A; D012697:Serine Endopeptidases; C000705287:PREPL protein, human; D000085822:Prolyl Oligopeptidases
vernacular_title: Proliléndopeptidaza II éritrotsitov cheloveka, gidrolizuiushchaia teprotid, ingibitor peptidil-dipeptidazy, iz zmeinogo iada.