Quantitative analysis of glycation patterns in human serum albumin using 16O/18O-labeling and MALDI–TOF MS

We developed a new method for MALDI-TOF MS detection of N-glycans derived from human serum. The synergistic combination of microwave-assisted Girard T derivatization, solid-phase extraction desalting, and an ionic liquid matrix (2, 5-dihydroxybenzoic acid/aniline) (GT-SPE-DHB/An) allowed of more sensitive N-glycans detection than a conventional ionic liquid matrix in MALDI-TOF MS. The superior sensitivity of our method was confirmed by the number of assigned N-glycans in 900–2,000 m/z range. Using our GT-SPE-DHB/An method, we were successfully able to assign 31 glycans. However, with the established method, i.e., DHB/An method, only 15 glycans were assigned. To the best of our knowledge, this GT-SPE-DHB/An method is the first to combine cationic derivatization of N-glycan and ionic liquid matrix for N-glycan analysis in MALDI-TOF MS.

Download Full-text

Characterization of Soluble Non-covalent Complexes between Bovine Serum Albumin and β-1,2,3,4,6-Penta-O-galloyl-d-glucopyranose by MALDI-TOF MS

Journal of Agricultural and Food Chemistry ◽

10.1021/jf035536t ◽

2004 ◽

Vol 52 (12) ◽

pp. 4008-4011 ◽

Cited By ~ 51

Author(s):

Yumin Chen ◽

Ann E. Hagerman

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Maldi Tof Ms ◽

Maldi Tof ◽

Tof Ms

Download Full-text

Analysis of site-specific N-homocysteinylation of human serum albumin in vitro and in vivo using MALDI-ToF and LC-MS/MS mass spectrometry

Journal of Proteomics ◽

10.1016/j.jprot.2011.01.021 ◽

2011 ◽

Vol 74 (7) ◽

pp. 967-974 ◽

Cited By ~ 20

Author(s):

Łukasz Marczak ◽

Marta Sikora ◽

Maciej Stobiecki ◽

Hieronim Jakubowski

Keyword(s):

Mass Spectrometry ◽

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Site Specific ◽

Maldi Tof

Download Full-text

Exploring adduct formation between human serum albumin and eleven organophosphate ester flame retardants and plasticizers using MALDI-TOF/TOF and LC-Q/TOF

Chemosphere ◽

10.1016/j.chemosphere.2017.03.124 ◽

2017 ◽

Vol 180 ◽

pp. 169-177 ◽

Cited By ~ 12

Author(s):

Shaogang Chu ◽

Margaret R. Baker ◽

Gladys Leong ◽

Robert J. Letcher ◽

Shirley J. Gee ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Flame Retardants ◽

Adduct Formation ◽

Maldi Tof

Download Full-text

Standardized Approach to Proteome Profiling of Human Serum Based on Magnetic Bead Separation and Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry

Clinical Chemistry ◽

10.1373/clinchem.2004.047308 ◽

2005 ◽

Vol 51 (6) ◽

pp. 973-980 ◽

Cited By ~ 171

Author(s):

Sven Baumann ◽

Uta Ceglarek ◽

Georg Martin Fiedler ◽

Jan Lembcke ◽

Alexander Leichtle ◽

...

Keyword(s):

Human Serum ◽

Mass Range ◽

Magnetic Bead ◽

Ionization Time ◽

Maldi Tof Ms ◽

Maldi Tof ◽

Flight Mass Spectrometry ◽

And Storage ◽

Magnetic Bead Separation ◽

Tof Ms

Abstract Background: Magnetic bead purification for the analysis of low-abundance proteins in body fluids facilitates the identification of potential new biomarkers by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). The aims of our study were to establish a proteome fractionation technique and to validate a standardized blood sampling, processing, and storage procedure for proteomic pattern analysis. Methods: We used magnetic bead separation for proteome profiling of human blood by MALDI-TOF MS (mass range, 1000–10 000 Da) and studied the effects on the quality and reproducibility of the proteome analysis of anticoagulants, blood clotting, time and temperature of sample storage, and the number of freeze–thaw cycles of samples. Results: The proteome pattern of human serum was characterized by ∼350 signals in the mass range of 1000–10 000 Da. The proteome profile showed time-dependent dynamic changes before and after centrifugation of the blood samples. Serum mass patterns differed between native samples and samples frozen once. The best reproducibility of proteomic patterns was with a single thawing of frozen serum samples. Conclusion: Application of the standardized preanalytical blood sampling and storage procedure in combination with magnetic bead-based fractionation decreases variability of proteome patterns in human serum assessed by MALDI-TOF MS.

Download Full-text