Bradykinin (BK)-like activity, which was detected by BK-enzyme-immunoa
ssay, was purified from 80 ml of ureter urine of Sprague-Dawley rats b
y Sephadex G 25 chromatography, FPLC, and reversed phase HPLC. The pur
ified kinin fraction showed the same retention time as authentic BK on
HPLC and produced contraction of isolated rat uterus, the contraction
being suppressed by a B2-antagonist Hoe140. There was no other kinin
detected on the HPLC at the corresponding retention time to kallidin,
arginyl-BK or T-kinin. The peptide showed an amino acid sequence ident
ical to that of BK by amino acid sequence analysis.