Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Metastable ion formation and disparate charge separation in the gas-phase dissection of protein assemblies studied by orthogonal time-of-flight mass spectrometry
Autore:
Versluis, C; van der Staaij, A; Stokvis, E; Heck, AJR; de Craene, B;
Indirizzi:
Univ Utrecht, Dept Biomol Mass Spectrometry, Bijvoet Ctr Biomol Res, NL-3584 CA Utrecht, Netherlands Univ Utrecht Utrecht Netherlands NL-3584 CA 3584 CA Utrecht, Netherlands Univ Utrecht, Utrecht Inst Pharmaceut Sci, NL-3584 CA Utrecht, NetherlandsUniv Utrecht Utrecht Netherlands NL-3584 CA 3584 CA Utrecht, Netherlands
Titolo Testata:
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
fascicolo: 3, volume: 12, anno: 2001,
pagine: 329 - 336
SICI:
1044-0305(200103)12:3<329:MIFADC>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTROSPRAY-IONIZATION; ESCHERICHIA-COLI; GLYOXALASE-I; DISSOCIATION; COMPLEXES; ENZYME;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Heck, AJR Univ Utrecht, Dept Biomol Mass Spectrometry, Bijvoet Ctr Biomol Res, Sorbonnelaan 16, NL-3584 CA Utrecht, Netherlands Univ Utrecht Sorbonnelaan 16 Utrecht Netherlands NL-3584 CA nds
Citazione:
C. Versluis et al., "Metastable ion formation and disparate charge separation in the gas-phase dissection of protein assemblies studied by orthogonal time-of-flight mass spectrometry", J AM SOC M, 12(3), 2001, pp. 329-336

Abstract

The dissection of specific and nonspecific protein complexes in the gas phase is studied by collisionally activated decomposition. In particular, thegas phase dissection of multiple protonated homodimeric Human Galectin I, E. Coli Glyoxalase I, horse heart cytochrome c, and Hen egg Lysozyme have been investigated. Both the Human Galectin I and E. Coli Glyoxalase I enzymes are biologically active as a dimer, exhibiting molecular weights of approximately 30 kDa. Cytochrome c and Lysozyme are monomers, but may aggregate to some extent at high protein concentrations. The gas phase dissociation of these multiple protonated dimer assemblies does lead to the formation of monomers. The charge distribution over the two concomitant monomers following the dissociation of these multiple protonated dimers is found to be highly dissimilar. There is no evident correlation between the solution phase stability of the dimeric proteins and their gas-phase dissociation pattern. Additionally, in the collisionally activated decomposition spectra diffuse ion signals are observed, which are attributed to monomer ions formed via slow decay of the collisionally activated dimer ions inside the reflection time-of-flight. Although, the formation of these diffuse metastable ions maycomplicate the interpretation of collisionally activated decomposition mass spectra, especially when studying noncovalent protein complexes, a simplemathematical equation may be used to reveal their origin and pathway of formation.(C) 2001 American Society for Mass Spectrometry.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 14:02:47