A novel method for analyzing phosphoproteins using SELDI-TOF MS in combination with a series of recombinant proteins.
A novel SELDI-TOF MS-based method for analyzing phosphoproteins was developed using a series of recombinant wild-type and mutant ribosomal P2 proteins. We demonstrated that the phosphorylation status of the overexpressed proteins in cells was easily and rapidly confirmed using this method. The ribosomal P2 protein contained two phosphorylation sites, which were sequentially phosphorylated in vivo. We also quantitatively detected the phosphoprotein by using SELDI-TOF MS.
Akashi
Tetsuyuki
T
Division of Molecular Pharmacology, Cancer Chemotherapy Center, Japanese Foundation for Cancer Research, Tokyo, Japan.
Yamori
Takao
T
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000032:analysis* / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000032:analysis / Q000737:chemistry / Q000235:genetics; D012269:Ribosomal Proteins / Q000737:chemistry; D016415:Sequence Alignment; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
D010750:Phosphoproteins; D011994:Recombinant Proteins; D012269:Ribosomal Proteins