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Measurement of relative amounts of phospho‐ and dephospho‐B‐50(GAP‐43) peptides by fast atom bombardment‐mass spectrometry
Author(s) -
Di Luca M.,
de Graan P.N.E.,
De Angelis L.,
Gispen W.H.,
Cattabeni F.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81236-f
Subject(s) - fast atom bombardment , mass spectrometry , chemistry , atom (system on chip) , analytical chemistry (journal) , chromatography , computer science , embedded system
The biological role of phosphoproteins depends upon their degree of phosphorylation in vivo. Methods currently available to measure the degree of phosphorylation of a protein involve indirect procedures to detect the 32 P‐phosphate incorporation. We report here a direct method to measure relative amounts of phospho‐ and dephospho‐forms of peptides based upon a mass spectrometric technique. The intensities of the molecular ions corresponding to the two forms of the peptides are proportional to their relative amounts. This is demonstrated for a peptide fragment of the protein B‐5O(GAP‐43) and for kemptide, respectively substrates for protein kinases C and A, and demonstrates the applicability of fast atom bombardment‐mass spectrometry to quantitate peptides bearing post‐translational modifications.