2008
DOI: 10.1016/j.chroma.2008.10.093
|View full text |Cite
|
Sign up to set email alerts
|

Proteomic approach for the analysis of acrylamide–hemoglobin adducts

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
10
0

Year Published

2009
2009
2020
2020

Publication Types

Select...
8

Relationship

0
8

Authors

Journals

citations
Cited by 9 publications
(11 citation statements)
references
References 54 publications
1
10
0
Order By: Relevance
“…Preston et al (2009) described the successful development of monoclonal antibodies specific for AA-adducted Hb, which was hoped by the authors to have potential for use in a high throughput analytical method; however this approach needs further development. Using MS/MS techniques to analyse whole globins or protein tryptic digests, Basile et al (2008) characterised the sites in Hb that form adducts with AA, and suggested that this proteomic approach to analyse these adducts has potential for use as a biomarker.…”
Section: Methodsmentioning
confidence: 99%
“…Preston et al (2009) described the successful development of monoclonal antibodies specific for AA-adducted Hb, which was hoped by the authors to have potential for use in a high throughput analytical method; however this approach needs further development. Using MS/MS techniques to analyse whole globins or protein tryptic digests, Basile et al (2008) characterised the sites in Hb that form adducts with AA, and suggested that this proteomic approach to analyse these adducts has potential for use as a biomarker.…”
Section: Methodsmentioning
confidence: 99%
“…Human dietary exposure to acrylamide through hemoglobin adduct determination has been carried out with various analytical methods. The standard method is based on the N-alkyl Edman degradation procedure to release the N-terminal Valine-acrylamide adduct which is then derivatised and determined by gas chromatography-mass spectrometry or liquid chromatography-mass spectrometry analysis [8].…”
Section: Introductionmentioning
confidence: 99%
“…The very high covalent binding in rat blood can be accounted for by the unusually high nucleophilic reactivity of the Cys-125␤ found in rat globin versus other vertebrate species (Neis et al, 1984;Miranda, 2000). Comparison of tryptic peptides between untreated and RRx-001-treated human Hb showed that Cys-␤93 is the dominant site of alkylation, analogous to reported alkylation by methyl bromide and acrylamide (Ferranti et al, 1996;Basile et al, 2008). Following the standard proteomic protocol of DTT reduction, the observed peptide adducts had exclusive adducts with the ketoazetidinyl and mononitroazetidinyl groups.…”
Section: Discussionmentioning
confidence: 74%