Proteomics approach to identifying ATP-covalently modified proteins.
This study aims to investigate functionally similar proteins based on their capacity to remain bound to ATP under stringent resolving conditions. Using two-dimensional gel electrophoresis and capillary liquid chromatography on-line mass spectrometry, we have identified several mammalian and E. coli proteins that appear to covalently bind ATP. To validate this approach, we obtained commercially purified forms of proteins identified from two-dimensional protein maps and tested their capacity to bind alpha 32P phosphate labeled ATP. This proteomics approach provides an initial screening method of identifying functionally similar proteins for further scrutiny by a more traditional analysis.
Department of Medicine, University of California-San Francisco, Parnassus, U-426, San Francisco, California 94143-0724, USA. pbesant@cyllene.uwa.edu.au
Paul G
PG
Besant
Michael V
MV
Lasker
Cuong D
CD
Bui
Eiling
E
Tan
Paul V
PV
Attwood
Christoph W
CW
Turck
D000255:Adenosine Triphosphate / Q000737:chemistry*; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D015180:Electrophoresis, Gel, Two-Dimensional; D029968:Escherichia coli Proteins / Q000032:analysis / Q000737:chemistry; D006801:Humans; D013058:Mass Spectrometry; D010759:Phosphorus Isotopes; D011506:Proteins / Q000032:analysis* / Q000737:chemistry*; D040901:Proteomics / Q000379:methods*
D029968:Escherichia coli Proteins; D010759:Phosphorus Isotopes; D011506:Proteins; D000255:Adenosine Triphosphate