Attomole protein characterization by capillary electrophoresis-mass spectrometry

Gary A. Valaskovic, Neil L. Kelleher, Fred W. McLafferty*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

332 Scopus citations


Electrospray ionization with an ultralow flow rate (≤4 nanoliters per minute) was used to directly couple capillary electrophoresis with tandem mass spectrometry for the analysis and identification of biomolecules in mixtures. A Fourier transform mass spectrometer provided full spectra (>30 kilodaltons) at a resolving power of ≃60,000 for injections of 0.7 x 10- 18 to 3 X 10-18 mole of 8- to 29-kilodalton proteins with errors of <1 dalton in molecular mass. Using a crude isolate from human blood, a value of 28,780.6 daltons (calculated, 28,780.4 daltons) was measured for carbonic anhydrase, representing 1 percent by weight of the protein in a single red blood cell. Dissociation of molecular ions from 9 x 10-18 mole of carbonic anhydrase gave nine sequence-specific fragment ions, more data than required for unique retrieval of this enzyme from the protein database.

Original languageEnglish (US)
Pages (from-to)1199-1202
Number of pages4
Issue number5279
StatePublished - 1996

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Attomole protein characterization by capillary electrophoresis-mass spectrometry'. Together they form a unique fingerprint.

Cite this