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Plasma desorption mass spectrometry of phosphopeptides: An investigation to determine the feasibility of quantifying the degree of phosphorylation
Author(s) -
Craig A. Grey,
Engström Åke,
Bennich Hans,
HoffmannPosorske Edeltraut,
Meyer Helmut E.
Publication year - 1991
Publication title -
biological mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1052-9306
DOI - 10.1002/bms.1200200910
Subject(s) - mass spectrometry , chemistry , desorption , mass spectrum , phosphorylation , analytical chemistry (journal) , ion , stoichiometry , residue (chemistry) , chromatography , spectral line , peptide , biochemistry , adsorption , organic chemistry , physics , astronomy
The intact ion yields of phosphotyrosine, phosphothreonine and mono‐ and diphosphoserine residue‐containing peptides have been compared with the non‐phosphorylated sequences using plasma desorption mass spectrometry. Equimolar mixtures of the phosphorylated (M P ) and non‐phosphorylated peptides (M) were also analysed. The positive mass spectra of these mixtures show a higher intensity of the [M + H] + compared with the [M P + H] + . In the negative mass spectrum, the bias towards the [M − H] − compared with the [M P − H] − was reduced, but the spectra generally did not accurately reflect the stoichiometry.