Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1995-3-29
pubmed:abstractText
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 degrees 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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
359
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
192-4
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The use of mass spectrometry to examine the formation and hydrolysis of the phosphorylated form of phosphoglycerate mutase.
pubmed:affiliation
Department of Biological and Molecular Sciences, University of Stirling, Scotland, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't