Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Aminopeptidases / isolation & purification*
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Animals
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Bradykinin
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Chromatography, Agarose
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Dipeptidyl Peptidase 4
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / isolation & purification
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Electrophoresis, Polyacrylamide Gel
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Lung / enzymology*
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Lysine Carboxypeptidase / isolation & purification*
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Microsomes / enzymology
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Rats
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Rats, Sprague-Dawley
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Substrate Specificity
Substances
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Aminopeptidases
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X-Pro aminopeptidase
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Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
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Dipeptidyl Peptidase 4
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Lysine Carboxypeptidase
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Bradykinin