Kislinger T, Humeny A, Becker CM, Peich C, Pischetsrieder M (2005)
Publication Type: Journal article
Publication year: 2005
Publisher: New York Academy of Sciences
Edited Volumes: Annals of the New York Academy of Sciences
Series: Annals of the New York Academy of Sciences
City/Town: New York
Book Volume: 1043
Pages Range: 249-259
Conference Proceedings Title: The Maillard Reaction. Chemistry at the Interface of Nutrition, Aging, and Disease
Event location: Charleston, South Carolina
ISBN: 1-57331-531-1
Matrix-assisted laser desorption ionization-mass spectrometry with time-of-flight detection (MALDI-TOF/MS) is a promising tool to analyze advanced glycation end product (AGE)-modified proteins. The combination of soft ionisation (MALDI) with time-of-flight mass detection allows analysis of peptides and proteins of a molecular mass up to 300 kDa with minimal sample workup. Because the direct structural analysis of intact AGE proteins is not possible due to the formation of broad and poorly resolved peaks, peptide mapping was introduced into the analysis of AGE proteins by MALDI-TOF/MS, allowing site-specific analysis of defined AGEs. When methylglyoxal-modified lysozyme was subjected to MALDI-TOF/MS peptide mapping, methylimidazolone and argpyrimidine attached to the arginine residue and carboxyethyl (CEL) bound to the lysine were detected on peptide
APA:
Kislinger, T., Humeny, A., Becker, C.-M., Peich, C., & Pischetsrieder, M. (2005). Analysis of Protein Glycation Products by MALDI-TOF/MS. Annals of the New York Academy of Sciences, 1043, 249-259. https://dx.doi.org/10.1196/annals.1333.030
MLA:
Kislinger, Thomas, et al. "Analysis of Protein Glycation Products by MALDI-TOF/MS." Annals of the New York Academy of Sciences 1043 (2005): 249-259.
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