| Literature DB >> 7643725 |
Y Hagiwara1, M Kojima, T Kuraishi, I Hayashi, T Miyata, S Oh-ishi.
Abstract
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.Entities:
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Year: 1995 PMID： 7643725 DOI： 10.1016/0024-3205(95)02035-h
Source DB: PubMed Journal: Life Sci ISSN： 0024-3205 Impact factor: 5.037