[Properties and action specificity of carboxycathepsin (peptidyl dipepsidase) from bovine kidneys].
Carboxycathepsin from bovine kidney split the dipeptide fragments from the C-terminal part of peptides of different structure. Peptides containing the proline residue at the second position from the C-terminal amino acid residue and also peptides with substituted terminal alpha-carboxyl group were not hydrolyzed by carboxycathepsin. The enzyme was activated by Cl, Zn2+, Co2+ and Mn2+. The substances which formed the chelate complexes with ions of two-valent metals and also heavy metal ions, inhibited the enzymatic activity. Diisopropyl fluorophosphate did not inhibit carboxycathepsin. The homogeneous preparation of carboxycathepsin converted angiotensin 1 into angiotensin 11 and hydrolyzed bradikinine, splitting off C-terminal dipeptides consequentially.
D000804:Angiotensin II / Q000378:metabolism; D000806:Angiotensin-Converting Enzyme Inhibitors; D000818:Animals; D001920:Bradykinin / Q000378:metabolism; D002417:Cattle; D002713:Chlorine / Q000494:pharmacology; D002855:Chromatography, Thin Layer; D003035:Cobalt / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D004589:Electrophoresis, Disc; D004591:Electrophoresis, Polyacrylamide Gel; D005470:Fluorometry / Q000379:methods; D006868:Hydrolysis; D007668:Kidney / Q000032:analysis; D007672:Kidney Cortex / Q000201:enzymology*; D008345:Manganese / Q000494:pharmacology; D010455:Peptides / Q000032:analysis / Q000378:metabolism; D007703:Peptidyl-Dipeptidase A / Q000032:analysis / Q000502:physiology*; D010618:Phenanthrolines / Q000494:pharmacology
D000806:Angiotensin-Converting Enzyme Inhibitors; D010455:Peptides; D010618:Phenanthrolines; D000804:Angiotensin II; D003035:Cobalt; D008345:Manganese; D002713:Chlorine; D004492:Edetic Acid; D007703:Peptidyl-Dipeptidase A; D001920:Bradykinin
Svoĭstva i spetsifichnost' deĭstviia karboksikatepsina (petidil-dipeptidazy) pochek byka