Document Detail


N-terminal glycation of proteins and peptides in foods and in vivo: evaluation of N-(2-furoylmethyl)valine in acid hydrolyzates of human hemoglobin.
MedLine Citation:
PMID:  18448804     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Specific determination of N-(2-furoylmethyl)valine (FM-Val) together with furosine in acid hydrolyzates of human hemoglobin of healthy volunteers (n = 6) and diabetic patients (n = 14) by means of reversed-phase HPLC with electrospray ionization-time-of-flight mass spectroscopy is reported. Whereas FM-Val is formed during acid hydrolysis of the N-terminal hemoglobin adduct N-fructosylvaline, furosine results from acid degradation of lysine residues glycated at the epsilon-amino group. Quantification was based on the use of synthesized isotopomers, namely N-[2-(13C6)furoylmethyl]valine and N-epsilon-[2-(13C6)furoylmethyl]lysine, thus enabling interference-free detection and calibration. Taking the conversion factors into account, the amount of N-terminally bound N-fructosylvaline in human hemoglobin was between 518 and 774 pmol/mg protein for healthy volunteers and between 586 and 1426 pmol/mg protein for diabetic patients. Derivatization at the side chain of peptide-bound lysine residues to N-epsilon-fructosyllysine was from 1156 to 1753 pmol/mg protein for healthy controls and from 1191 to 2409 pmol/mg protein for diabetics. For these patients, the amount of N-fructosylvaline showed good correlation with the values for HbA(1c). The significantly higher relative extent of glycation at the N terminus compared to side-chain glycation points to a specific and intraindividual capacity for enzymatic deglycation in human erythrocytes, which can be assessed using the proposed method.
Authors:
Ilka Penndorf; Changhao Li; Uwe Schwarzenbolz; Thomas Henle
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Annals of the New York Academy of Sciences     Volume:  1126     ISSN:  0077-8923     ISO Abbreviation:  Ann. N. Y. Acad. Sci.     Publication Date:  2008 Apr 
Date Detail:
Created Date:  2008-05-01     Completed Date:  2008-08-12     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7506858     Medline TA:  Ann N Y Acad Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  118-23     Citation Subset:  IM    
Affiliation:
Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany.
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MeSH Terms
Descriptor/Qualifier:
Blood Proteins / chemistry
Chromatography, High Pressure Liquid
Food Analysis*
Glycosylation End Products, Advanced
Hemoglobin A, Glycosylated / analysis
Hemoglobins / chemistry*
Humans
Lysine / analogs & derivatives,  analysis
Peptides / chemistry*
Proteins / chemistry*
Spectrometry, Mass, Electrospray Ionization
Valine / analogs & derivatives*,  analysis*
Chemical
Reg. No./Substance:
0/Blood Proteins; 0/Glycosylation End Products, Advanced; 0/Hemoglobin A, Glycosylated; 0/Hemoglobins; 0/N-(2-furoylmethyl)valine; 0/Peptides; 0/Proteins; 21291-40-7/fructosyl-lysine; 56-87-1/Lysine; 7004-03-7/Valine

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