Triacylglycerol profile in cocoa liquors using MALDI-TOF and LC-ESI tandem mass spectrometry

2014 ◽  
Vol 49 (9) ◽  
pp. 894-899 ◽  
Author(s):  
Luca Bono ◽  
Roberta Seraglia ◽  
Marco Roverso ◽  
Marina Di Carro ◽  
Emanuele Magi
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Tandem Mass ◽  
Maldi Tof ◽  
Triacylglycerol Profile

scholarly journals MALDI-TOF/TOF Tandem Mass Spectrometry Imaging Reveals Non-uniform Distribution of Disaccharide Isomers in Plant Tissues

2020 ◽  
Author(s):  
lingpeng zhan ◽  
xi huang ◽  
jinjuan xue ◽  
huihui liu ◽  
caiqiao xiong ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Mass Spectrometry Imaging ◽  
Biological Tissues ◽  
Plant Tissues ◽  
Tandem Mass ◽  
Imaging Analysis ◽  
Maldi Tof ◽  
Ms Imaging ◽  
Imaging Approach

Mass spectrometry imaging (MSI) has been increasingly utilized in investigating the locations of biomolecules within tissues. However, the isomeric compounds are rarely distinguished in the MS images, due to inability of MSI methods to differentiate isomers in the probing area. Coupling tandem mass spectrometry with MSI can facilitate differentiating isomeric compounds in ion images. Here we apply MALDI-TOF/TOF tandem mass spectrometry imaging approach to revealing the spatial distributions of isomeric disaccharides in plant tissues. First, the MS/MS imaging analysis of disaccharide-matrix droplet spots demonstrated the feasibility of distinguishing isomeric species in tissues, by measuring the relative intensity of specific fragments. Then, we conducted tandem MS imaging of disaccharides in onion bulb tissues, which indicated that sucrose and other unknown non-sucrose disaccharides exhibit heterogeneous locations throughout the tissues. This method enables us to image disaccharide isomers differentially in biological tissues, and to discover new saccharide species in plant. This work also emphasizes the necessity of considering isobaric compounds when interpreting MSI results.<br>

Profiling microcystin contamination in a water reservoir by MALDI-TOF and liquid chromatography coupled to Q/TOF tandem mass spectrometry

2013 ◽  
Vol 54 (1) ◽  
pp. 1321-1330 ◽  
Author(s):  
Pasquale Ferranti ◽  
Serena Fabbrocino ◽  
Eugenio Chiaravalle ◽  
Milena Bruno ◽  
Adriana Basile ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Liquid Chromatography ◽  
Tandem Mass Spectrometry ◽  
Water Reservoir ◽  
Tandem Mass ◽  
Maldi Tof

scholarly journals Identification of 2D-gel proteins: A comparison of MALDI/TOF peptide mass mapping to μ LC-ESI tandem mass spectrometry

2003 ◽  
Vol 14 (9) ◽  
pp. 957-970 ◽  
Author(s):  
Hanjo Lim ◽  
Jimmy Eng ◽  
John R. Yates ◽  
Sandra L. Tollaksen ◽  
Carol S. Giometti ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Tandem Mass ◽  
Maldi Tof ◽  
Peptide Mass ◽  
Mass Mapping ◽  
2D Gel

scholarly journals Comparison of methods to examine the endogenous peptides of fetal calf serum

2021 ◽  
Author(s):  
Declan Williams ◽  
Peihong Zhu ◽  
Peter Bowden ◽  
Catherine Stacey ◽  
Mike McDonell ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Sample Preparation ◽  
Tandem Mass Spectrometry ◽  
Amino Acid Substitutions ◽  
Tandem Mass ◽  
Preparation Methods ◽  
Endogenous Peptides ◽  
Maldi Tof ◽  
Sample Preparation Methods

There is a great desire to relate the patterns of endogenous peptides in blood to human disease and drug response. The best practices for the preparation of blood fluids for analysis are not clear and also relatively few of the peptides in blood have been identified by tandem mass spectrometry. We compared a number of sample preparation methods to extract endogenous peptides including C18 reversed phase, precipitation, and ultrafiltration. We examined the results of these sample preparation methods by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-tandem mass spectrometry (MS/MS) using MALDI-TOF/TOF and electrospray ionization-ion trap. Peptides from solid-phase extraction with C18 in the range of hundreds of femtomoles per spot were detected from the equivalent of 1 μL of serum by MALDI-TOF. We observed endogenous serum peptides from fibrinogen α- and β-chain, complement C3, α-2-HS-glycoprotein, albumin, serine (or cysteine) proteinase inhibitor, factor VIII, plasminogen, immunoglobulin, and other abundant blood proteins. However, we also recorded significant MS/MS spectra from tumor necrosis factor-α-, major histocompatibility complex-, and angiotensin-related peptides, as well as peptides from collagens and other low-abundance proteins. Amino acid substitutions were detected and a phosphorylated peptide was also observed. This is the first time the endogenous peptides of fetal serum have been examined by MS and where peptides from low-abundance proteins, phosphopeptides, and amino acid substitutions were detected.

Structural Characterization of Oligosaccharides Using Maldi-TOF/TOF Tandem Mass Spectrometry

2003 ◽  
Vol 75 (18) ◽  
pp. 4895-4903 ◽  
Author(s):  
Yehia Mechref ◽  
Milos V. Novotny ◽  
Cheni Krishnan
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Structural Characterization ◽  
Tandem Mass ◽  
Maldi Tof

Identification of the over alkylation sites of a protein by IAM in MALDI-TOF/TOF tandem mass spectrometry

RSC Advances ◽  
2015 ◽  
Vol 5 (125) ◽  
pp. 103662-103668 ◽  
Author(s):  
Mengzhe Guo ◽  
Guofeng Weng ◽  
Dengyang Yin ◽  
Xunxiu Hu ◽  
Jie Han ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Disulfide Bonds ◽  
Side Chain ◽  
Tandem Mass ◽  
Proteolytic Digestion ◽  
Digestion Process ◽  
Maldi Tof

Overalkylation often appears during the proteolytic digestion process when using iodoacetamide (IAM) to protect the produced side chain thiol of Cys from disulfide bonds.

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