Degradation of bradykinin by isolated neutral endopeptidases of brain and pituitary
Review articleOpen access

AbstractThe degradation of bradykinin by a highly purified preparation of rabbit brain prolyl endopeptidase and by an apparently homogeneous preparation of a bovine pituitary cation-sensitive neutral endopeptidase was studied. Peptide fragments were separated and isolated by high performance liquid chromatography and identified by amino acid analysis. Prolyl endopeptidase rapidly cleaves bradykinin at the Pro7-Phe8 bond. A slower cleavage also occurs at the Pro3-Gly4 bond. Cation-sensitive neutral endopeptidase splits bradykinin at the Phe5-Ser6 bond. These enzymes may participate in the regulation of brain concentrations of bradykinin.

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