Abstract
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 language | English (US) |
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Pages (from-to) | 1199-1202 |
Number of pages | 4 |
Journal | Science |
Volume | 273 |
Issue number | 5279 |
DOIs | |
State | Published - 1996 |
ASJC Scopus subject areas
- General