中国科学院大连化学物理研究所机构知识库
Advanced  
DICP OpenIR  > 中国科学院大连化学物理研究所  > 会议论文
学科主题: 物理化学
题名: Isolation and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from red deer plasma
作者: Liu XY(刘晓燕) ;  Jin Y(靳艳) ;  Zou HF(邹汉法)
会议名称: The 24th International Symposium on Micro-scale Bioseparation,
会议日期: 2009-10-19
出版日期: 2009-10-19
会议地点: 中国
通讯作者: 邹汉法
部门归属: 十八室
主办者: 大连化学物理研究所
摘要: Hypertension is a significant health problem worldwide, which carries a high risk factor for cardiovascular and cerebrovascular disease. It is estimated that about 20% of the worldwide adult population suffers from this common serious chronic disease. Angiotensin I-converting enzyme (ACE) inhibitor is one of the antihypertensive drugs, such as captopril, alacepril and enalapril. ACE, which plays an important role in regulating blood pressure, catalyzes the conversion of angiotensin from an inactive decapeptide (angiotensinⅠ) to a potent vasoconstrictor octapeptide (angiotensinⅡ) and inactivates antihypertensive vasodilator bradykinin. Various ACE inhibitory drugs have been shown to result in an antihypertensive effect, but these artificially synthesized ACE inhibitors are believed to have certain side effects, such as cough, angioedema, taste disturbance and skin rashes. Therefore, bioactive peptides with ACE inhibitory activity derived from food proteins are considered to be safer and have no side effects for treatment of hypertension. The blood of deer is used as traditional Chinese medicine for a long time. In this study, a novel peptide with ACE inhibitory was stemmed from red deer plasma. Red deer plasma protein was precipitated by acetone and subsequently digested. The separation was performed with Sephadex G-25 gel filtration chromatography. The fraction with highest ACE inhibitory activity was analyzed by electrospray ionization tandem mass spectrometry (ESI-MS/MS). ESI-MS/MS data and modeling structure information were used to search for ACE inhibitory peptides in red deer database. A novel inhibitory effect peptide with sequence VYNEGLPAP was firstly obtained from red deer plasma. The 50% inhibition concentration (IC50) was 3.1 μM in vitro. Stability study for ACE inhibitory activity showed that this nonapeptide had the good heat and pH stability and strong enzyme-resistant properties against gastrointestinal protease. Kinetic experiments demonstrated that inhibitory kinetic mechanism of this peptide was competitive. These results suggest that the nonapeptide and the hydrolysate from red deer plasma proteins may be potential source with antihypertensive effect. Keywords: Angiotensin I-converting enzyme; Inhibitory activity; Peptide; Red deer plasma
语种: 中文
内容类型: 会议论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/113836
Appears in Collections:中国科学院大连化学物理研究所_会议论文

Files in This Item:

There are no files associated with this item.


Recommended Citation:
Liu XY,Jin Y,Zou HF. Isolation and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from red deer plasma[C]. 见:The 24th International Symposium on Micro-scale Bioseparation,. 中国. 2009-10-19.
Service
 Recommend this item
 Sava as my favorate item
 Show this item's statistics
 Export Endnote File
Google Scholar
 Similar articles in Google Scholar
 [刘晓燕]'s Articles
 [靳艳]'s Articles
 [邹汉法]'s Articles
CSDL cross search
 Similar articles in CSDL Cross Search
 [刘晓燕]‘s Articles
 [靳艳]‘s Articles
 [邹汉法]‘s Articles
Related Copyright Policies
Null
Social Bookmarking
  Add to CiteULike  Add to Connotea  Add to Del.icio.us  Add to Digg  Add to Reddit 
所有评论 (0)
暂无评论
 
评注功能仅针对注册用户开放,请您登录
您对该条目有什么异议,请填写以下表单,管理员会尽快联系您。
内 容:
Email:  *
单位:
验证码:   刷新
您在IR的使用过程中有什么好的想法或者建议可以反馈给我们。
标 题:
 *
内 容:
Email:  *
验证码:   刷新

Items in IR are protected by copyright, with all rights reserved, unless otherwise indicated.

 

 

Valid XHTML 1.0!
Powered by CSpace