1993
DOI: 10.1016/0009-8981(93)90168-4
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Studies on zinc and angiotensin-converting enzyme

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Cited by 6 publications
(2 citation statements)
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“…3.4.15.1), also known as kininase II, is a zinc-requiring metalloenzyme. 4 It is a membrane-bound glycoprotein, localized mainly in the endothelial cells of pulmonary capillaries. ACE catalyzes the cleavage of histidyl-leucine from the carboxyl-terminal of AI, yielding an octapeptide angiotensin II (AII), and it inactivates bradykinin.…”
Section: Introductionmentioning
confidence: 99%
“…3.4.15.1), also known as kininase II, is a zinc-requiring metalloenzyme. 4 It is a membrane-bound glycoprotein, localized mainly in the endothelial cells of pulmonary capillaries. ACE catalyzes the cleavage of histidyl-leucine from the carboxyl-terminal of AI, yielding an octapeptide angiotensin II (AII), and it inactivates bradykinin.…”
Section: Introductionmentioning
confidence: 99%
“…The solution was ultracentrifuged at 100,000 g for 20 min and the supernatant was dialyzed overnight with 10 mM HEPES buffer, pH 7.5, containing 0.3 M KCI and 100 pM ZnCh (2 x 2 liters). 50 pl of dialyzed solution were assayed for ACE activity evaluated by FAPGG hydrolytic activity, following the kinetic ACE methods as proposed (4). Ovary Triton-X100 extraction, protease inhibitors were added immediately to the homogenized sample: PMSF (500 pM), pepstatin (1 pM), leupeptin (5 pM) and antipain (25 pM) (final concentrations) and the resulting pellet after ultracentrifugation at 100,000 g for 20 min was resuspended in 4 ml of phosphate buffer with all the protease inhibitors and Triton-X100 was added to a final concentration of 1% (v/v) (16).…”
Section: Methodsmentioning
confidence: 99%