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Titolo:
Transfer of SDS-proteins from gel electrophoretic zones into mass spectrometry, using electroelution of the band into buffer without sectioning of the gel
Autore:
Yefimov, S; Yergey, AL; Chrambach, A;
Indirizzi:
NICHD, Macromol Anal Sect, Lab Cellular & Mol Biophys, NIH, Bethesda, MD 20892 USA NICHD Bethesda MD USA 20892 ar & Mol Biophys, NIH, Bethesda, MD 20892 USA NICHD, Sect Mass Spectrometry & Metab, Lab Cellular & Mol Biophys, NIH, Bethesda, MD 20892 USA NICHD Bethesda MD USA 20892 ar & Mol Biophys, NIH, Bethesda, MD 20892 USA
Titolo Testata:
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS
fascicolo: 1-2, volume: 42, anno: 2000,
pagine: 65 - 78
SICI:
0165-022X(20000103)42:1-2<65:TOSFGE>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
HPGE-1000 APPARATUS; RESOLUTION; SYSTEM; FIELD; SENSITIVITY; RECOVERY;
Keywords:
mass spectrometry; real-time scanning; fluorescent proteins; electroeluates; HPGE apparatus;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Chrambach, A NICHD, Macromol Anal Sect, Lab Cellular & Mol Biophys, NIH, Bldg 10,Room 9D50, Bethesda, MD 20892 USA NICHD Bldg 10,Room 9D50 Bethesda MD USA 20892 a, MD 20892 USA
Citazione:
S. Yefimov et al., "Transfer of SDS-proteins from gel electrophoretic zones into mass spectrometry, using electroelution of the band into buffer without sectioning of the gel", J BIOCH BIO, 42(1-2), 2000, pp. 65-78

Abstract

Five SDS-proteins, ranging in molecular weight from 14 to 66 kDa, were detected without covalent fluorescent labeling by the automated gel electrophoresis apparatus with intermittent fluorescence scanning (HPGE apparatus, LabIntelligence) during electrophoresis in barbiturate buffer in the presenceof Cascade Blue. The SDS-proteins were electroeluted from the gel into 220mu l of buffer by a modification of the procedure of Gombocz and Cortez [1]. The electroeluate was freed of SDS, ultrafiltered and subjected to MALDI-TOF mass spectrometry. The masses of the five native proteins were found to be maintained after electrophoresis and electroelution in the presence ofthe potential contaminants SDS, barbituric acid and Cascade Blue. The procedure of protein transfer from SDS-PAGE into mass spectrometry, without excision of bands, gel maceration and protein recovery by diffusion, thereforeis shown to be suitable for the identification by mass of intact proteins derived from gel electrophoretic bands. (C) 2000 Elsevier Science BN. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 22:20:09