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Titolo:
Monitoring 2-D gel-induced modifications of proteins by MALDI-TOF mass spectrometry
Autore:
Hamdan, M; Galvani, M; Righetti, PG;
Indirizzi:
GlaxoSmithKline Grp, Med Res Ctr, I-37135 Verona, Italy GlaxoSmithKline Grp Verona Italy I-37135 Res Ctr, I-37135 Verona, Italy Univ Verona, Dept Agr & Ind Biotechnol, I-37100 Verona, Italy Univ VeronaVerona Italy I-37100 & Ind Biotechnol, I-37100 Verona, Italy
Titolo Testata:
MASS SPECTROMETRY REVIEWS
fascicolo: 3, volume: 20, anno: 2001,
pagine: 121 - 141
SICI:
0277-7037(200105/06)20:3<121:M2GMOP>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
SODIUM DODECYL-SULFATE; ASSISTED LASER DESORPTION/IONISATION; TIME-OF-FLIGHT; IMMOBILINE CHEMICALS; POLYACRYLAMIDE GELS; HEMOGLOBIN ADDUCTS; BETA-LACTOGLOBULIN; SEPARATED PROTEINS; ELECTROPHORESIS; ACRYLAMIDE;
Keywords:
MALDI-TOF MS; protein modifications; N-substituted acrylamides; immobilines; gel crosslinkers; 2-D maps;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Hamdan, M GlaxoSmithKline Grp, Med Res Ctr, Via Fleming 4, I-37135 Verona,Italy GlaxoSmithKline Grp Via Fleming 4 Verona Italy I-37135 a, Italy
Citazione:
M. Hamdan et al., "Monitoring 2-D gel-induced modifications of proteins by MALDI-TOF mass spectrometry", MASS SPECTR, 20(3), 2001, pp. 121-141

Abstract

In addition to more than 200 endogenously produced posttranslational modifications, a detailed analysis of 2-D gel-separated proteins must also consider other modifications that a protein can experience during various steps of its separation. This review describes the use of matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry to investigate some of these modifications, which can originate during sample preparation and/or during the separation phase. The analyses described were mostly conducted at pH 9-9.5, and yielded reliable information on stable adduct formation that involved protein-bound amino acids and a number of gel components, including acrylamide derivatives, gel cross-linkers, and Immobiline chemicals. The -SH group of Cys was found to be the prime target of such adducts; however, longer reaction times revealed the involvement of the epsilon -NH2 of Lys. The same analysis revealed that the failure to achieve fullreduction/alkylation prior to any electrophoretic step could result in protein - protein interaction, which could lead to a number of spurious spots in the final 2-D map. The implications of these modifications on the MS analysis in particular and on proteome research in general are discussed. (C) 2001 John Wiley & Sons, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 15:32:17