Aminopeptidase P: purification of a membrane-bound bradykininase from rat lung.
Aminopeptidase P that hydrolyzes the Arg1-Pro2-bond of bradykinin was solubilized from rat lung microsomes using phosphatidylinositol-specific phospholipase C. The enzyme was purified 420-fold by chromatography on decylagarose (two steps), omega-aminodecyl-agarose and DEAE-Sephacel. A single stained band was observed following native gradient (4-15%) polyacrylamide gel electrophoresis. Dipeptidylaminopeptidase IV-like activity was also present in the final preparation and co-migrated with aminopeptidase P in the above gel system.
Department of Molecular and Cellular Biochemistry, Loyola University of Chicago Stritch School of Medicine, Maywood, IL 60153.
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Orawski
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Simmons
D000626:Aminopeptidases / Q000302:isolation & purification*; D000818:Animals; D001920:Bradykinin; D002847:Chromatography, Agarose; D018819:Dipeptidyl Peptidase 4; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D008168:Lung / Q000201:enzymology*; D001121:Lysine Carboxypeptidase / Q000302:isolation & purification*; D008861:Microsomes / Q000201:enzymology; D051381:Rats; D017207:Rats, Sprague-Dawley; D013379:Substrate Specificity
D000626:Aminopeptidases; C022750:X-Pro aminopeptidase; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D018819:Dipeptidyl Peptidase 4; D001121:Lysine Carboxypeptidase; D001920:Bradykinin