期刊
PEPTIDES
卷 30, 期 6, 页码 1028-1033出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2009.03.002
关键词
Acaudina molpadioidea; Angiotensin I-converting enzyme inhibitory peptide; Antihypertensive effect; Spontaneously hypertensive rat
资金
- 863 Research Program, China [2006AA09Z438]
Body wall protein from the sea cucumber (Acaudina molpadioidea) was hydrolyzed sequentially with bromelain and alcalase. The hydrolysate was fractionated into two ranges of molecular weight (PH-I, >2 kDa; PH-II, <2 kDa) using an ultrafiltration membrane bioreactor system. The PH-II brought about a high angiotensin I-converting enzyme (ACE) inhibitory activity. An ACE inhibitory peptide was isolated from the PH-II, using the chromatographic methods including gel filtration, ion-exchange chromatography and reversed phase high-performance liquid chromatography. The purified ACE inhibitory peptide was a novel peptide, showing very low similarity to other ACE inhibitory peptide sequences, and was sequenced as MEGAQEAQGD. It was found that the inhibitory activity of the peptide was intensified by 3.5 times from IC50 15.9 to IC50 4.5 mu M after incubation with gastrointestinal proteases. The ACE inhibitory peptide from A. molpadioidea showed a clear anti hypertensive effect in spontaneously hypertensive rats (SHR), at a dosage of 3 mu M/kg. (C) 2009 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据