Linked Life Data

16690189

Source:http://linkedlifedata.com/resource/pubmed/id/16690189

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2006-6-23
pubmed:abstractText
Oxidised lipids are reported to interact with proteins causing undesirable changes in nutritional and functional properties including a loss of amino acids, cross-linking and damage to proteins and DNA. ESR spectroscopy with spin trapping was used to study the type of radical species generated in methyl linoleate and the transfer of the radical to protein beta-lactoglobulin. Antioxidants vitamins C and E reduced lipid oxidation and subsequent transfer of the radical to the protein as shown by the shape and size of the radical adduct. Changes to protein molecular structure due to oxidation were investigated by multidimensional NMR spectroscopy and liquid chromatography. NMR spectra indicated that as a result of oxidation and protein denaturation, there was an increase in structural flexibility and some initially protected backbone amide groups were exposed as they become sharper and easily identifiable. Dityrosine was detected in all samples tested which is indicative of oxidative damage to proteins. Monitoring tyrosyl radicals and formation of dityrosine is of practical value in order to enhance the acceptability, nutritional and safety aspects of proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0278-6915
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1385-92
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
ESR and NMR spectroscopy studies on protein oxidation and formation of dityrosine in emulsions containing oxidised methyl linoleate.
pubmed:affiliation
School of Biomedical and Molecular Sciences, University of Surrey, Guildford, Surrey GU2 7XH, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't