Linked Life Data

20045374

Source:http://linkedlifedata.com/resource/pubmed/id/20045374

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-2-4
pubmed:abstractText
Hydroxyl radicals generated from Fenton reaction were used to damage the angiotensin. The oxidative damage degree and sites of peptides were measured by HPLC-MS and MS/MS. Experimental results proved that the oxidative damage degree increased with longer reaction time. The results also showed that the side chains of phenylalanine and tyrosine in angiotension can be attacked by hydroxyl radicals to form the oxidative products. A new strategy was established to monitor the oxidative degree and sites of peptides and laid the foundation for protein oxidation. This method can be used to investigate the mechanism of protein oxidative damage caused by oxidative stress which is induced by environmental pollutants and physiological activities. There will also be a wide application in the research of pathogenesis of some disease related to oxidative stress.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1873-3557
pubmed:author
pubmed:copyrightInfo
Copyright (c) 2010 Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
908-11
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
A new biomarker of protein oxidation degree and site using angiotensin as the target by MS.
pubmed:affiliation
School of Environmental Science and Engineering, Shandong University, 27 Shanda South Road, Jinan 250100, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't