Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
ATTOMOLE PROTEIN CHARACTERIZATION BY CAPILLARY ELECTROPHORESIS MASS-SPECTROMETRY
Autore:
VALASKOVIC GA; KELLEHER NL; MCLAFFERTY FW;
Indirizzi:
CORNELL UNIV,BAKER LAB,DEPT CHEM ITHACA NY 14853 CORNELL UNIV,BAKER LAB,DEPT CHEM ITHACA NY 14853
Titolo Testata:
Science
fascicolo: 5279, volume: 273, anno: 1996,
pagine: 1199 - 1202
SICI:
0036-8075(1996)273:5279<1199:APCBCE>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
MULTIPLY-CHARGED IONS; ELECTROSPRAY-IONIZATION; LARGE BIOMOLECULES; LARGE MOLECULES; SENSITIVITY; PEPTIDES; SPECTRA; IDENTIFICATION; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
G.A. Valaskovic et al., "ATTOMOLE PROTEIN CHARACTERIZATION BY CAPILLARY ELECTROPHORESIS MASS-SPECTROMETRY", Science, 273(5279), 1996, pp. 1199-1202

Abstract

Electrospray ionization with an ultralow flow rate (less than or equal to 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 ofapproximate to 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 28,780.6daltons (calculated, 28,780.4 daltons) was measured for carbonic anhydrase, representing 1 percent by weight of the protein in a single redblood cell. Dissociation of molecular ions from 9 x 10(-18) mole of carbonic anhydrase gave nine sequence-specific fragment ions, more datathan required for unique retrieval of this enzyme from the protein database.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 12:22:28