Angiotensin converting enzyme in brush-border membranes of avian small intestine.
Angiotensin converting enzyme activity was identified in brush-border membranes purified from the small intestinal epithelium of the common grackle, Quiscalus quiscula. Angiotensin converting enzyme was enriched 20-fold in the membrane preparation, compared with intestinal epithelial cell scrapes, and was coenriched with the brush-border markers, alkaline phosphatase and aminopeptidase N. The kinetics of hydrolysis of N-[3-(2-furyl)acryloyl]-L-phenylalanylglycylglycine (FAPGG) gave a Vmax of 907 +/- 41 units g-1 and a Km of 55 +/- 6 mumol l-1. The avian intestinal angiotensin converting enzyme was inhibited by the antihypertensive drug, Ramipril, with a median inhibitory concentration (IC50) of 1 nmol l-1. In the light of previous studies on angiotensin converting enzyme in mammalian epithelia, these results may implicate a physiological role for angiotensin converting enzyme in regulating electrolyte and fluid uptake in bird small intestines.
Stevens
B R
BR
Department of Physiology, College of Medicine, University of Florida, Gainesville 32610.
Fernandez
A
A
Martinez del Rio
C
C
D000818:Animals; D001717:Birds / Q000378:metabolism*; D007413:Intestinal Mucosa / Q000201:enzymology; D007421:Intestine, Small / Q000201:enzymology*; D007700:Kinetics; D008871:Microvilli / Q000201:enzymology*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*
D007703:Peptidyl-Dipeptidase A