Identification of rat urinary kinin as bradykinin.
Bradykinin (BK)-like activity, which was detected by BK-enzyme-immunoassay, was purified from 80 ml of ureter urine of Sprague-Dawley rats by Sephadex G 25 chromatography, FPLC, and reversed phase HPLC. The purified 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 identical to that of BK by amino acid sequence analysis.
Hagiwara
Y
Y
Department of Pharmacology, School of Pharmaceutical Sciences, Kitasato University, Tokyo, Japan.
Kojima
M
M
Kuraishi
T
T
Hayashi
I
I
Miyata
T
T
Oh-ishi
S
S
D000595:Amino Acid Sequence; D000818:Animals; D001681:Biological Assay; D001920:Bradykinin / Q000031:analogs & derivatives / Q000737:chemistry / Q000494:pharmacology / Q000652:urine*; D002851:Chromatography, High Pressure Liquid; D005260:Female; D008297:Male; D008969:Molecular Sequence Data; D051381:Rats; D017207:Rats, Sprague-Dawley; D017421:Sequence Analysis; D014590:Uterine Contraction / Q000187:drug effects
C065679:icatibant; D001920:Bradykinin