Central action of Bradykinin (II) Separation of Bradykinin degrading enzyme from the rat brain.

Abstract
Separation of kininases from the rat brain and identification of the products produced by these enzymes were examined using DEAE-cellulose column chromatography and thin-layer chromatography, respectively. Fraction A (F-A), which was developed with 70 mM NaCl, released Arg-Pro-Pro-Gly-Phe and Ser-Pro-Phe-Arg, fraction B (F-B), with 100 mM NaCl, cleaved the Pro7-Phe8 and Phe8-Arg9 peptide bonds of the bradykinin molecule and fraction C (F-C) with 150 mM NaCl hydrolyzed bradykinin to amino acids. The specific activity of each fraction determined by the bioassay system was 158.7, 51.0 and 14.8 nmole bradykinin/mg protein/ min, respectively. The intensities of their fluorescence on the chromatogram showed visibly that o-phenanthroline effectively inhibited F-A, B and C at a concentration of 0.5 mM. These results suggest that heterogeneous enzyme systems are present in the rat brain and regulate the levels of bradykinin in the brain.

This publication has 1 reference indexed in Scilit: