Identification of phosphorylated proteins from thrombin-activated human platelets isolated by two-dimensional gel electrophoresis by electrospray ionization-tandem mass spectrometry (ESI-MS/MS) and liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS)

1998 ◽  
Vol 19 (6) ◽  
pp. 1015-1023 ◽  
Author(s):  
Dorian Immler ◽  
Dagmar Gremm ◽  
Dieter Kirsch ◽  
Bernhard Spengler ◽  
Peter Presek ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Ionization ◽  
Gel Electrophoresis ◽  
Human Platelets ◽  
Ionization Mass ◽  
Tandem Mass ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Esi Ms ◽  
Phosphorylated Proteins

Characterization of wheat gliadin proteins by combined two-dimensional gel electrophoresis and tandem mass spectrometry

PROTEOMICS ◽  
2005 ◽  
Vol 5 (11) ◽  
pp. 2859-2865 ◽  
Author(s):  
Gianfranco Mamone ◽  
Francesco Addeo ◽  
Lina Chianese ◽  
Aldo Di Luccia ◽  
Alessandra De Martino ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Gel Electrophoresis ◽  
Tandem Mass ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Wheat Gliadin

Characterization of Electrospray Ionization Mass Spectrometry for N-Diisopropyloxyphosphoryl Dipeptide Methyl Esters

2005 ◽  
Vol 11 (1) ◽  
pp. 107-117 ◽  
Author(s):  
Shi-Zhong Luo ◽  
Yan-Mei Li ◽  
Yan-Ling Niu ◽  
Yi Chen ◽  
Yu-Yang Jiang ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Tandem Mass Spectrometry ◽  
Electrospray Ionization ◽  
Metal Ion ◽  
Methyl Esters ◽  
Ionization Mass ◽  
Tandem Mass ◽  
Fragmentation Pattern ◽  
Esi Ms

A systematic study of the fragmentation pattern of N-diisopropyloxyphosphoryl (DIPP) dipeptide methyl esters in an electrospray ionization (ESI) tandem mass spectrometry (MS/MS) was presented. A combination of accurate mass measurement and tandem mass spectrometry had been used to characterize the major fragment ions observed in the ESI mass spectrum. It was found that the alkali metal ions acted as a fixed charge site and expelled the DIPP group after transferring a proton to the amide nitrogen. For all the N-phosphoryl dipeptide methyl esters, under the activation of a metal ion, the rearrangement product ion at m/z 163 was observed and confirmed to be the sodium adduct of phosphoric acid mono-isopropyl esters (PAIE), via a specific five-membered penta-coordinated phosphorus intermediate. However, no rearrangement ion was observed when a β-amino acid was at the N-terminal. This could be used to develop a novel method for differentiating isomeric compounds when either α- or β-amino acid are at the N-terminus of peptides. From the [M + Na]+ ESI-MS/MS spectra of N-phosphoryl dipeptide methyl esters (DIPP – Xaa1 – Xaa2 – OMe), the peaks corresponding to the [M + Na – Xaa1 – C3H6]+ were observed and explained. The [M + Na]+ ESI-MS/MS spectra of N-phosphoryl dipeptide methyl esters with Phe located in the C-terminal, such as DIPP–Val–Phe–OMe, DIPP–Leu–Phe–OMe, DIPP–Ile–Phe–OMe, DIPP–Ala–Phe–OMe and DIPP–Phe–Phe–OMe, had characteristic fragmentation. Two unusual gas-phase intramolecular rearrangement mechanisms were first proposed for this fragmentation. These rearrangements were not observed in dipeptide methyl ester analogs which did not contain the DIPP at the N-terminal, suggesting that this moiety was critical for the rearrangement.

Proteomic profiling of sea bass muscle by two-dimensional gel electrophoresis and tandem mass spectrometry

2013 ◽  
Vol 40 (1) ◽  
pp. 311-322 ◽  
Author(s):  
Genciana Terova ◽  
Salvatore Pisanu ◽  
Tonina Roggio ◽  
Elena Preziosa ◽  
Marco Saroglia ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Gel Electrophoresis ◽  
Sea Bass ◽  
Tandem Mass ◽  
Two Dimensional ◽  
Proteomic Profiling ◽  
Two Dimensional Gel Electrophoresis
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