Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2003-1-3
pubmed:abstractText
Two methods based on specific immunoaffinity enrichment followed by electrospray ionization (ESI) mass spectrometry (MS) have been developed for the specific analysis of 4-hydroxy-2-nonenal (HNE)- and malondialdehyde (MDA)-modified proteins (Michael and Schiff base adducts, respectively). Anti-HNE antibodies were immobilized on CNBr-activated sepharose, and the immunosorbent produced was used for the enrichment of HNE-adducted peptides originating from a model peptide modification and a tryptic digest of modified apomyoglobin. A further immunosorbent was produced by anti-dinitrophenyl immobilization and assayed for selective extraction of peptides modified with HNE and MDA that were initially converted to their respective hydrazones. Subsequent analysis and characterization of the different purified fractions by ESI-MS (MS/MS) revealed that the two immunosorbents enable efficient and specific enrichment of the carbonyl adducted proteins. This approach lowers substantially the detection limit of such modifications and, thus, enables better assessment and characterization of carbonyl modifications in biological and food systems.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0003-2700
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6298-304
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Immunoaffinity purification and characterization of 4-hydroxy-2-nonenal- and malondialdehyde-modified peptides by electrospray ionization tandem mass spectrometry.
pubmed:affiliation
Department of Quality and Safety Assurance, Nestle Research Center, Nestec Ltd., Vers-Chez-les-Blanc, 1000 Lausanne 26, Switzerland.
pubmed:publicationType
Journal Article