Kinin cleavage by human erythrocytes

An aminopeptidase‐P has been purified 230‐fold from human erythrocytes. The purified enzyme cleaved arginine from des‐(Arg9)‐bradykinin (Arg‐Pro‐Pro‐Gly‐Phe‐Ser‐Pro‐Phe) had a molecular weight in nondenaturing buffers of 155,000 ± 6,900 daltons, was not inactivated by chelating agents, had a pH opti...

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Veröffentlicht in:	American journal of hematology 1984-01, Vol.17 (4), p.383-391
Hauptverfasser:	Sidorowicz, W., Canizaro, Peter C., Běhal, Francis J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aminoacids, peptides. Hormones. Neuropeptides Aminopeptidases - isolation & purification Aminopeptidases - metabolism Aminopeptidases - pharmacology aminopeptidase‐P Analytical, structural and metabolic biochemistry Arginine - metabolism Biological and medical sciences bradykinin Bradykinin - analogs & derivatives Bradykinin - metabolism Dipeptides - metabolism Edetic Acid - pharmacology Enzyme Activation Erythrocyte Membrane - enzymology erythrocytes Erythrocytes - enzymology Erythrocytes - physiology Female Fundamental and applied biological sciences. Psychology Humans kinin cleavage kininase Kinins - metabolism Male Metals - pharmacology Peptide Fragments - isolation & purification Peptide Fragments - metabolism Proteins
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