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Titolo:
Protein identification by in-gel digestion, high-performance liquid chromatography, and mass spectrometry: Peptide analysis by complementary ionization techniques
Autore:
Medzihradszky, KF; Leffler, H; Baldwin, MA; Burlingame, AL;
Indirizzi:
Univ Calif San Francisco, Sch Pharm, Dept Pharmaceut Chem, Mass Spectrometry Facil, San Francisco, CA 94143 USA Univ Calif San Francisco San Francisco CA USA 94143 ancisco, CA 94143 USA Univ Lund, Dept Clin Immunol, S-22362 Lund, Sweden Univ Lund Lund SwedenS-22362 d, Dept Clin Immunol, S-22362 Lund, Sweden
Titolo Testata:
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
fascicolo: 2, volume: 12, anno: 2001,
pagine: 215 - 221
SICI:
1044-0305(200102)12:2<215:PIBIDH>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
SEQUENCE DATABASES; ELECTROSPRAY IONIZATION; DEAMIDATION; EVOLUTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Burlingame, AL Univ Calif San Francisco, Sch Pharm, Dept Pharmaceut Chem, Mass Spectrometry Facil, 521 Parnassus Ave, San Francisco, CA 94143 USA Univ Calif San Francisco 521 Parnassus Ave San Francisco CA USA 94143
Citazione:
K.F. Medzihradszky et al., "Protein identification by in-gel digestion, high-performance liquid chromatography, and mass spectrometry: Peptide analysis by complementary ionization techniques", J AM SOC M, 12(2), 2001, pp. 215-221

Abstract

A biologically active protein fraction was isolated from rabbit intestine,purified by one-dimensional SDS-PAGE and stained with Coomassie Brilliant Blue. A predominant band of approximately 110-130 kDa was excised and digested in-gel with trypsin. The resulting peptides were extracted then separated by microbore reversed-phase high-performance liquid chromatography (HPLC). Mass spectrometric data from one HPLC fraction obtained by two differentionization techniques proved to be complementary. Matrix-assisted laser desorption/ ionization (MALDI) showed nine peptide masses, which by post source decay analysis and database searching were attributed to two proteins. Nanoflow electrospray analysis performed on a hybrid tandem mass spectrometer of quadrupole- quadrupole- orthogonal acceleration time-of-flight (QqTOF)geometry detected six additional peptide components. On the basis of the additional peptides and superior quality collision-induced dissociation spectra typical of this instrument type, two further proteins were identified. The resolution afforded by the QqTOF instrument permitted charge state determination for the fragment ions while preserving the high detection sensitivity that was essential in obtaining the composition of this mixture of proteins. (C) 2001 American Society for Mass Spectrometry.

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Documento generato il 10/04/20 alle ore 02:01:58