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Titolo:
Protein alkylation by acrylamide, its N-substituted derivatives and cross-linkers and its relevance to proteomics: A matrix assisted laser desorption/ionization-time of flight-mass spectrometry study
Autore:
Hamdan, M; Bordini, E; Galvani, M; Righetti, PG;
Indirizzi:
Univ Verona, Dept Agr & Ind Biotechnol, I-37134 Verona, Italy Univ VeronaVerona Italy I-37134 & Ind Biotechnol, I-37134 Verona, Italy GlaxoSmithKline Grp, Med Res Ctr, Verona, Italy GlaxoSmithKline Grp Verona Italy hKline Grp, Med Res Ctr, Verona, Italy
Titolo Testata:
ELECTROPHORESIS
fascicolo: 9, volume: 22, anno: 2001,
pagine: 1633 - 1644
SICI:
0173-0835(200105)22:9<1633:PABAIN>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
OF-FLIGHT; IMMOBILINE CHEMICALS; POLYACRYLAMIDE GELS; HEMOGLOBIN ADDUCTS; ELECTROPHORESIS; CYSTEINE; KINETICS; SITES;
Keywords:
protein alkylation; immobiline chemicals; N-substituted acrylamides; cross-linkers; matrix assisted laser desorption; ionization-time of flight-mass spectrometry; review;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Righetti, PG Univ Verona, Dept Agr & Ind Biotechnol, Strada Grazie 15, I-37134 Verona, Italy Univ Verona Strada Grazie 15 Verona Italy I-37134 ona, Italy
Citazione:
M. Hamdan et al., "Protein alkylation by acrylamide, its N-substituted derivatives and cross-linkers and its relevance to proteomics: A matrix assisted laser desorption/ionization-time of flight-mass spectrometry study", ELECTROPHOR, 22(9), 2001, pp. 1633-1644

Abstract

The present review highlights some important alkylation pathways of proteins, as measured by matrix assisted laser desorption/ionization-time of flight (MALDI-TOF)-mass spectrometric analysis, engendered by acrylamide and a number of its derivatives, including N-substituted acrylamides, cross-linkers and Immobilines (the acrylamido weak acids and bases used to create immobilized pH gradients). The present data are of relevance in two-dimensionalmaps and proteome analysis. It is shown that acrylamide can alkylate the -SH group of proteins even when engaged in disulfide bridges. An order of reactivity is obtained for a series of cross-linkers, which are shown to havean extremely reacting double bond, with the second one almost unreactive, originating "pendant, unreacted ends", which can subtract proteins migrating in a gel by covalently affixing them to it. An analogous reactivity scaleis constructed also for the Immobiline chemicals, whose reactivity is shown to be linearly dependent on the pK values, the least reacting species being the acidic compounds. When analyzing real-life samples by two-dimensional (2-D) maps, like milk powders, a number of modifications can be detected by MALDI-TOF mass spectra of eluted spots, including variable phosphorylation sites (up to nine) and lactosyl moieties. If, for eluting such spots, formic acid is used, MALDI-TOF mass spectrometry (MS) reveals an incredible number of formylation sites, on Ser and Thr residues.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 12:56:42