Attomole quantitation of protein separations with accelerator mass spectrometry

John S. Vogel, Patrick G. Grant, Bruce A. Buchholz, Karen Dingley, Ken W Turteltaub

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


Quantification of specific proteins depends on separation by chromatography or electrophoresis followed by chemical detection schemes such as staining and fluorophore adhesion. Chemical exchange of short-lived isotopes, particularly sulfur, is also prevalent despite the inconveniences of counting radioactivity. Physical methods based on isotopic and elemental analyses offer highly sensitive protein quantitation that has linear response over wide dynamic ranges and is independent of protein conformation. Accelerator mass spectrometry quantifies long-lived isotopes such as 14C to sub-attomole sensitivity. We quantified protein interactions with small molecules such as toxins, vitamins, and natural biochemicals at precisions of 1-5%. Micro-proton-induced X-ray emission quantifies elemental abundances in separated metalloprotein samples to nanogram amounts and is capable of quantifying phosphorylated loci in gels. Accelerator-based quantitation is a possible tool for quantifying the genome translation into proteome.

Original languageEnglish (US)
Pages (from-to)2037-2045
Number of pages9
Issue number10
StatePublished - 2001
Externally publishedYes


  • Accelerator mass spectrometry
  • Protein
  • Proteome
  • Quantitation
  • Radioisotope
  • Review

ASJC Scopus subject areas

  • Clinical Biochemistry


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