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- W4243662856 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 NaCI, released Arg-Pro-Pro-Gly-Phe and Ser-Pro-Phe-Arg, fraction B (F-B), with 100 mM NaCI, cleaved the Pro7-Phe8 and Phe8-Arg9 peptide bonds of the brady-kinin molecule and fraction C (F-C) with 150 mM NaCI hydrolyzed brady-kinin to amino acids. The specific activity of each fraction determined by the bioassay system was 1 58.7, 51.0 and 14.8 nmole bradykinin/mg protein/min, respectively. The intensities of their fluorescence on the chromato-gram 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 brady-kinin in the brain." @default.
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- W4243662856 date "1981-01-01" @default.
- W4243662856 modified "2023-10-18" @default.
- W4243662856 title "CENTRAL ACTION OF BRADYKININ (II) SEPARATION OF BRADYKININ DEGRADING ENZYME FROM THE RAT BRAIN" @default.
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- W4243662856 doi "https://doi.org/10.1016/s0021-5198(19)52825-6" @default.
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