Results 151 to 160 of about 6,277 (184)
[Isolation and properties of carboxycathepsin (peptidyl-dipeptidase) from bovine lung tissue].
Biokhimiia (Moscow, Russia), 1976 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.
Eliseeva IuE +2 more
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Journal of Neurochemistry, 1990 Abstract: Incubation of various authentic peptides with rat CSF in vitro and analysis of their products by HPLC demonstrated the presence in CSF of a peptidyl dipeptidase [peptidyl dipeptide hydrolase; angiotensin I converting enzyme (ACE); kininase II; EC 3.4.15.1] which sequentially degraded bradykinin (BK) by liberating the carboxy‐terminal ...
Takeshi Yoshida, Shoichiro Nosaka
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Voprosy meditsinskoi khimii, 1984 Properties of the carboxycathepsin inhibitors teprotide, captopryl, enalacryl are considered. Presence of low molecular thermo- and acid stable carboxycathepsin inhibitors of peptide nature in blood serum and lymphocytes is discussed.
Orekhovich Vn +4 more
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