• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Life sciences >Thimet oligopeptidase EC 3.4.24.15 is a major liver kininase.
【24h】

Thimet oligopeptidase EC 3.4.24.15 is a major liver kininase.

机译：Thimet寡肽酶EC 3.4.24.15是主要的肝脏激肽酶。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Bradykinin (BK) is a potent hepato-portal hypertensive agent although it is efficiently inactivated by the liver. The organ converts angiotensin I to AII, but at a much slower rate than it inactivates BK. We had previously identified EC 3.4.24.15 as an hepatic bradykinin inactivating endopeptidase that hydrolyzes BK at the F5-F6 bond. The aim of this study was to determine the relative importance of BIE, as compared to other kininases, in normal, cirrhotic or inflamed rat livers, as well as in samples of human liver. Using specific substrates and inhibitors we showed that: 1) purified BIE preparation hydrolyzed BK and a BK analogue (BK-Q) with similar efficacy; BK-Q was functionally active since it caused an increase in hepato-portal pressure, as did BK itself. 2) BK degradation in rat serum was performed by ACE since BIE and prolylendopeptidase (PEP) activities were negligible. 3) normal rat liver homogenate contained a large amount of BIE activity which was eliminated by a specific EC 3.4.24.15 inhibitor; ACE and PEP activities were negligible. 4) There was no difference (p>0.05) in BIE activity in the liver homogenates from rats with normal, inflamed or cirrhotic livers. 5) BIE activity was efficiently removed from livers (normal, inflamed or cirrhotic) that were perfused with TritonX-100.6) Human liver had an similar enzymatic pattern although ACE activity was detected. We concluded that in normal, inflamed or cirrhotic rat livers, as well as in the human liver, the bradykinin inactivating endopeptidase (EC 3.4.24.15), and not ACE, is the major hepatic kininase.
机译：缓激肽（BK）是一种有效的肝门高血压药物，尽管它可以被肝脏有效地灭活。该器官将血管紧张素I转化为AII，但速率比灭活BK慢得多。我们之前已经确定EC 3.4.24.15是一种肝缓激肽失活的内肽酶，它能水解F5-F6键处的BK。这项研究的目的是确定在正常，肝硬化或发炎的大鼠肝脏以及人肝样品中，与其他激肽酶相比，BIE的相对重要性。使用特定的底物和抑制剂，我们表明：1）纯化的BIE制剂水解BK和具有相似功效的BK类似物（BK-Q）; BK-Q具有功能活性，因为它引起肝门压力的升高，就像BK本身一样。 2）由于BIE和脯氨酸肽酶（PEP）的活性可忽略不计，因此通过ACE在大鼠血清中进行BK降解。 3）正常大鼠肝脏匀浆含有大量的BIE活性，该活性被特定的EC 3.4.24.15抑制剂消除。 ACE和PEP活动微不足道。 4）正常，发炎或肝硬化大鼠的肝匀浆的BIE活性没有差异（p> 0.05）。 5）有效地从灌注TritonX-100.6的肝脏（正常，发炎或肝硬化）中去除BIE活性）尽管检测到ACE活性，但人类肝脏具有相似的酶促模式。我们得出的结论是，在正常的，发炎的或肝硬化的大鼠肝脏以及人的肝脏中，缓激肽失活的内肽酶（EC 3.4.24.15）而不是ACE是主要的肝激肽酶。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号