Hagiwara Y, Kojima M, Kuraishi T, Hayashi I, Miyata T, Oh-ishi S
Department of Pharmacology, School of Pharmaceutical Sciences, Kitasato University, Tokyo, Japan.
Life Sci. 1995;57(10):997-1002. doi: 10.1016/0024-3205(95)02035-h.
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.
通过葡聚糖凝胶G 25柱色谱、快速蛋白质液相色谱(FPLC)和反相高效液相色谱(HPLC),从80毫升斯普拉格-道利大鼠输尿管尿液中纯化出用缓激肽酶免疫测定法检测到的类缓激肽(BK)活性物质。纯化的激肽组分在HPLC上与标准BK具有相同的保留时间,并能使离体大鼠子宫收缩,该收缩可被B2拮抗剂Hoe140抑制。在与赖氨酰缓激肽、精氨酰-BK或T-激肽相应保留时间的HPLC上未检测到其他激肽。通过氨基酸序列分析,该肽显示出与BK相同的氨基酸序列。