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The best ionization efficiency of gallic and ellagic acid in the negative-ion MS mode was registered when the concentration of formic acid in the eluent equaled 0.10%.
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Because of the relatively low stoichiometric nature and ionization efficiency of phosphopeptides in mass spectrometric analysis, an efficient enrichment step is strongly recommended in phosphoproteomic studies.
It presents a raw ionization efficiency of 2.5 × 10−3.
In addition, mobile phase with high organic solvent ratio increased the ionization efficiency of LS.
A range of ionization efficiency of 1 2.5% was obtained by optimizing the described parameters.
The ionization efficiency of the plasma source permits the study of a wide range of elements.
The ionization efficiency of peptides resulting from derivatization was enhanced 10 100 fold, depending on the peptide sequence and hydrophobicity of the ionization tag.
Furthermore, the ionization efficiency of the βGC protein was significantly reduced at low concentrations.
However, in this specific case, it appears that PG (17:0/17:0) enhances the ionization efficiency of diplopterol.
Mass spectrometry is not a quantitative technique as the signal intensities depend on the ionization efficiency of the respective molecule.
The absence of signals for peptide RNA conjugates was attributed to low ionization efficiency of then negatively charged species.
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