http://www.cnr.it/ontology/cnr/individuo/prodotto/ID51149
The reductive desulfurization of Met and Cys residues in bovine RNAse A associated with the trans lipid formation in a mimetic model of biological membranes (Articolo in rivista)
- Type
- Label
- The reductive desulfurization of Met and Cys residues in bovine RNAse A associated with the trans lipid formation in a mimetic model of biological membranes (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Alternative label
Ferreri, C.; Chatgilialoglu, C.; Torreggiani, A.; Salzano, A. M.; Renzone, G.; Scaloni, A (2008)
The reductive desulfurization of Met and Cys residues in bovine RNAse A associated with the trans lipid formation in a mimetic model of biological membranes
in Journal of proteome research (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Ferreri, C.; Chatgilialoglu, C.; Torreggiani, A.; Salzano, A. M.; Renzone, G.; Scaloni, A (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- ISOF, Consiglio Nazionale delle Ricerche, via P. Gobetti 101, 40129 Bologna, Italy,
and Proteomics & Mass Spectrometry Laboratory, ISPAAM, Consiglio Nazionale delle Ricerche, via Argine 1085, 80147 Napoli, Italy (literal)
- Titolo
- The reductive desulfurization of Met and Cys residues in bovine RNAse A associated with the trans lipid formation in a mimetic model of biological membranes (literal)
- Abstract
- Damage to bovine pancreatic RNase A, due to the Ho atom and/or solvated electron attack at protein
sulfur-containing residues, was investigated by Raman spectroscopy and mass spectrometry techniques.
To the already known desulfurization process affecting Met residues, novel reactivity was observed
involving disulfide moieties, leading to the chemical transformation of Cys into Ala residues. Mapping
experiments demonstrated that desulfurization selectively affected Met79, Cys110, Cys58 and Cys72
during first stages of reaction. While this reaction was performed on protein species added to large
unilamellar vescicles, desulfurization yielded sulfur radicals able to induce a cis-trans isomerization of
lipids at the onset of irradiation. These findings reveal new scenarios on reactions generated by radical
stressing conditions, suggesting the need for specific assays and for future investigations to detect
these modifications in proteins and lipids within challenged cells. (literal)
- Prodotto di
- Autore CNR
Incoming links:
- Prodotto
- Autore CNR di
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi