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Characteristics of glycation and glycation sites of lysozyme by matrix-assisted laser desorption/ionization time of flight/time-of-flight mass spectrometry and Liquid chromatography-electrospray ionization tandem mass spectrometry.
Eur J Mass Spectrom (Chichester). 2014; 20(4):327-36.EJ

Abstract

Protein glycation with reducing sugars through the Maillard reaction is regarded as one of the most important reactions in food chem- istry. Amadori rearrangement products [ARPs] are produced at the initial stage of the Maillard reaction and then advanced glycation products may be formed. We report here that using matrix-assisted laser desorption/ionization mass spectrometry with time-of-flight detection [MALDI-TOF-MS] and electrospray ionization mass spectrometry (ESI-MSJ to monitor the glycation process in lysozyme and the D-glucose model system. MALDI-TOF-MS displayed a heterogeneous distribution of glycation via a total mass shift in spectra. However electrospray ionization mass spectrometry [ESI-MS] data showed that a total of four molecules of glucose reacted with Lysozyme at an increase in molecular weight by a 162 Da unit. Further, we identified the glycation sites of lysozyme by using MALDI-TOF/TOF-MS and Liquid chromatography [LC]-ESI-MS/MS. Besides the two glycation sites of Lys1 and Lys97 identified by MALDI-TOF/TOF-MS, the other two glycation sites of Lys13 and Lys116 were characterized unambiguously by LC-ESI-MS/MS. Both MALDI-TOF/TOF-MS and LC-ESI-MS/ MS provided confidence in the study of the glycation by restricting the number of possible residues through (un]modified ions. The study is useful to monitor and characterize glycation in protein systems based on both MALDI-TOF-MS and ESI-MS. Comparatively, LC-ESI-MS/MS provides more fragments with better recovery for the identification of glycation than MALDI-TOF/TOF-MS.

Authors

Ruan ED
No affiliation info available
Wang H
No affiliation info available
Ruan Y
No affiliation info available
Juáreza M
No affiliation info available

MeSH

Amino Acid SequenceChromatography, LiquidGlycosylationMolecular Sequence DataMuramidaseSpectrometry, Mass, Electrospray IonizationSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

25420345

Citation

Ruan, Eric Dongliang, et al. "Characteristics of Glycation and Glycation Sites of Lysozyme By Matrix-assisted Laser Desorption/ionization Time of Flight/time-of-flight Mass Spectrometry and Liquid Chromatography-electrospray Ionization Tandem Mass Spectrometry." European Journal of Mass Spectrometry (Chichester, England), vol. 20, no. 4, 2014, pp. 327-36.
Ruan ED, Wang H, Ruan Y, et al. Characteristics of glycation and glycation sites of lysozyme by matrix-assisted laser desorption/ionization time of flight/time-of-flight mass spectrometry and Liquid chromatography-electrospray ionization tandem mass spectrometry. Eur J Mass Spectrom (Chichester). 2014;20(4):327-36.
Ruan, E. D., Wang, H., Ruan, Y., & Juáreza, M. (2014). Characteristics of glycation and glycation sites of lysozyme by matrix-assisted laser desorption/ionization time of flight/time-of-flight mass spectrometry and Liquid chromatography-electrospray ionization tandem mass spectrometry. European Journal of Mass Spectrometry (Chichester, England), 20(4), 327-36.
Ruan ED, et al. Characteristics of Glycation and Glycation Sites of Lysozyme By Matrix-assisted Laser Desorption/ionization Time of Flight/time-of-flight Mass Spectrometry and Liquid Chromatography-electrospray Ionization Tandem Mass Spectrometry. Eur J Mass Spectrom (Chichester). 2014;20(4):327-36. PubMed PMID: 25420345.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characteristics of glycation and glycation sites of lysozyme by matrix-assisted laser desorption/ionization time of flight/time-of-flight mass spectrometry and Liquid chromatography-electrospray ionization tandem mass spectrometry. AU - Ruan,Eric Dongliang, AU - Wang,Hui, AU - Ruan,Yuanyuan, AU - Juáreza,Manuel, PY - 2014/11/26/entrez PY - 2014/11/26/pubmed PY - 2015/5/30/medline SP - 327 EP - 36 JF - European journal of mass spectrometry (Chichester, England) JO - Eur J Mass Spectrom (Chichester) VL - 20 IS - 4 N2 - Protein glycation with reducing sugars through the Maillard reaction is regarded as one of the most important reactions in food chem- istry. Amadori rearrangement products [ARPs] are produced at the initial stage of the Maillard reaction and then advanced glycation products may be formed. We report here that using matrix-assisted laser desorption/ionization mass spectrometry with time-of-flight detection [MALDI-TOF-MS] and electrospray ionization mass spectrometry (ESI-MSJ to monitor the glycation process in lysozyme and the D-glucose model system. MALDI-TOF-MS displayed a heterogeneous distribution of glycation via a total mass shift in spectra. However electrospray ionization mass spectrometry [ESI-MS] data showed that a total of four molecules of glucose reacted with Lysozyme at an increase in molecular weight by a 162 Da unit. Further, we identified the glycation sites of lysozyme by using MALDI-TOF/TOF-MS and Liquid chromatography [LC]-ESI-MS/MS. Besides the two glycation sites of Lys1 and Lys97 identified by MALDI-TOF/TOF-MS, the other two glycation sites of Lys13 and Lys116 were characterized unambiguously by LC-ESI-MS/MS. Both MALDI-TOF/TOF-MS and LC-ESI-MS/ MS provided confidence in the study of the glycation by restricting the number of possible residues through (un]modified ions. The study is useful to monitor and characterize glycation in protein systems based on both MALDI-TOF-MS and ESI-MS. Comparatively, LC-ESI-MS/MS provides more fragments with better recovery for the identification of glycation than MALDI-TOF/TOF-MS. SN - 1469-0667 UR - https://www.unboundmedicine.com/medline/citation/25420345/Characteristics_of_glycation_and_glycation_sites_of_lysozyme_by_matrix_assisted_laser_desorption/ionization_time_of_flight/time_of_flight_mass_spectrometry_and_Liquid_chromatography_electrospray_ionization_tandem_mass_spectrometry_ DB - PRIME DP - Unbound Medicine ER -
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