The use of mass spectrometry to examine the formation and hydrolysis of the phosphorylated form of phosphoglycerate mutase

Citation

Nairn J, Krell T, Coggins JR, Pitt AR, Fothergill-Gilmore LA, Walter RA & Price NC (1995) The use of mass spectrometry to examine the formation and hydrolysis of the phosphorylated form of phosphoglycerate mutase. FEBS Letters, 359 (2-3), pp. 192-194. https://doi.org/10.1016/0014-5793%2895%2900044-A

Abstract
Electrospray mass spectrometry has been used to study the formation and hydrolysis of the phosphorylated forms of two phosphoglycerate mutases. The half-life of the enzyme from Saccharomyces cerevisiae was 35 min at 20°C in 10 mM ammonium bicarbonate, pH 8.0. Addition of 1 mM 2-phosphoglycollate reduced this value by at least 100-fold. The phosphorylated form of the enzyme from Schizosaccharomyces pombe was much less stable with a half-life of less than 1 min. The results are discussed in terms of the kinetic properties of the enzymes. Mass spectrometry would appear to be a powerful method to study the formation and breakdown of phosphorylated proteins, processes which are of widespread significance in regulatory mechanisms.

Keywords
Electrospray mass spectrometry; Protein phosphorylation; Phosphoglycerate mutase

Notes
Output Type: Letter

Journal
FEBS Letters: Volume 359, Issue 2-3