PubMed:16212443 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/16212443","sourcedb":"PubMed","sourceid":"16212443","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/16212443","text":"Optimizing thiophosphorylation in the presence of competing phosphorylation with MALDI-TOF-MS detection.\nThiophosphorylation provides a metabolically stable, chemically reactive phosphorylation analogue for analyzing the phosphoproteome in vitro and in vivo. We developed a MALDI-TOF-MS based assay for optimizing thiophosphopeptide production by a kinase even in the presence of Mg(2+) and ATP. We found that Abl kinase thiophosphorylation rates can be \"rescued\" using Mn(2+) in the presence of Mg(2+). Under our ideal conditions, titration of Mn(2+) and ATPgammaS in the presence of Mg(2+) allowed relatively rapid, highly specific thiophosphorylation by Abl tyrosine kinase, both as purified enzyme and in complex cell 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