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- W2416129906 abstract "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." @default.
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- W2416129906 date "1976-03-01" @default.
- W2416129906 modified "2023-09-23" @default.
- W2416129906 title "[Isolation and properties of carboxycathepsin (peptidyl-dipeptidase) from bovine lung tissue]." @default.
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