The purpose of the present study was to contrast a commonly used ACE inhibitor (enalaprilat) with a novel ACE inhibitor (trandolaprilat) in their ability to inhibit 1) pulmonary capillary endothelialbound ACE activity in vivo, 2) arterial pressure responses to i.v. angiotensin I and bradykinin, and
Assay of Pulmonary Microvascular Endothelial Angiotensin-Converting Enzyme in Vivo: Comparison of Three Probes
β Scribed by S.E. Orfanos; X.L. Chen; J.W. Ryan; A.Y.K. Chung; S.E. Burch; J.D. Catravas
- Book ID
- 112265623
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 912 KB
- Volume
- 124
- Category
- Article
- ISSN
- 0041-008X
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## Abstract Angiotensinβconverting enzyme (EC 3.4.15.1) is a carboxyterminal dipeptidyl peptidase. The enzyme catalyzes the conversion of the decapeptide angiotensin I to the octapeptide angiotensin II. In addition, the enzyme catabolizes bradykinin. Because of these actions, the enzyme is of pivot
We estimated the activity of pulmonary capillary endothelium-bound (PCEB) angiotensin converting enzyme (ACE) in the rabbit in vivo, before and at 20 min and 2 h postadministration of the ACE inhibitors trandolaprilat (8 Β΅g/kg) and enalaprilat (10 Β΅g/kg), alone and in combination with the calcium ch