VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Properties and action specificity of carboxycathepsin (peptidyl dipepsidase) from bovine kidneys

   
Eliseeva I.E., Orekhovich V.N., Pavlikhina L.V.
PubMed Id: 193290
Year: 1976  Volume: 22  Issue: 1  Pages: 81-89
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.
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Citation:

Eliseeva, I. E., Orekhovich, V. N., Pavlikhina, L. V. (1976). Properties and action specificity of carboxycathepsin (peptidyl dipepsidase) from bovine kidneys. Voprosy Meditsinskoi Khimii, 22(1), 81-89.
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