Angiotensin I Converting Enzyme (Kininase II) of the Brush Border of Human and Swine Intestine.
Abstract
Mucosal brush border of human and swine small intestine is rich in angiotensin I converting enzyme or kininase II (ACE). The brush border of the intestinal mucosa was purified by centrifugation over a discontinuous glycerol gradient. Transmission electron micrographs showed that 90% of the isolated vesicles had a trilaminar membrance structure and glycocalix, characteristic to intestinal brush border. No significant contamination by other subcellular particles was evident. In the final purfied preparation the brush border marker enzymes sucrase, trehalase, and alkaline phosphatase were enriched 23, 18 and 17 fold from human intestine and 27, 26 and 20 fold from swine tissue. ACE was highly concentrated in the human and swine brush border. The specific activity of ACE in the human and swine brush border fractions was enriched 17 and 7.6 fold over the crude homogenate. Kininase activity was demonstrated by biosassy. These studies were also prompted by the use of the specific inhibitor of ACE, SQ 14225 or captopril, on a large scale in experimental animals and in hypertensive patients (11 - 14). Since this drug is given orally, it may inhibit ACE in the intestinal tract even before reaching the enzyme elsewhere in the organism.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 23, 1980
- Accession Number
- ADA086296
Entities
People
- Ervin G. Erdoes
- Katy J. Hammon
- Martha A. Sheridan
- Patrick E. Ward
Organizations
- University of Texas at Austin