[Isolation and properties of carboxycathepsin (peptidyl-dipeptidase) from bovine lung tissue].
2200-fold purified homogenous preparation of carboxycathepsin (peptidyl-dipeptidase) is isolated from bovine lung. The enzyme isolated converts angiotensine I into angiotensine II and distroys bradikinin. It is active in neutral medium, is activated by chloride ion and is inhibited by EDTA and Middle Asian snakes venom. The molecular weight of the enzyme is 180 000-190 000 as estimated by means of polyacrylamide gel electrophoresis, its isoelectric point is 4.48-4.53. The comparison of properties and specificity of carboxycathepsin from bovine lung and kidney draws to the conclusion that both enzymes are identical.
D000806:Angiotensin-Converting Enzyme Inhibitors; D000818:Animals; D002384:Catalysis; D002417:Cattle; D002713:Chlorine; D004492:Edetic Acid; D007525:Isoelectric Focusing; D008168:Lung / Q000201:enzymology*; D008970:Molecular Weight; D010455:Peptides; D007703:Peptidyl-Dipeptidase A / Q000302:isolation & purification; D012910:Snake Venoms
D000806:Angiotensin-Converting Enzyme Inhibitors; D010455:Peptides; D012910:Snake Venoms; D002713:Chlorine; D004492:Edetic Acid; D007703:Peptidyl-Dipeptidase A
Vydelenie i svoĭstva karboksikatepsina (peptidil-dipeptidazy) iz tkani legkikh byka