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Titolo:
Reactive carbonyl formation by oxidative and non-oxidative pathways
Autore:
Adams, S; Green, P; Claxton, R; Simcox, S; Williams, MV; Walsh, K; Leeuwenburgh, C;
Indirizzi:
Univ Florida, Biochem Aging Lab, Gainesville, FL 32611 USA Univ Florida Gainesville FL USA 32611 ging Lab, Gainesville, FL 32611 USA
Titolo Testata:
FRONTIERS IN BIOSCIENCE
, volume: 6, anno: 2001,
pagine: A17 - A24
SICI:
1093-9946(200108)6:<A17:RCFBOA>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOW-DENSITY-LIPOPROTEIN; HUMAN ATHEROSCLEROTIC INTIMA; PROTEIN OXIDATION; PLASMA-PROTEINS; CATALYZED OXIDATION; CIGARETTE-SMOKE; DAMAGE; PEROXYNITRITE; GLUTATHIONE; DITYROSINE;
Keywords:
aging; 2,4-dinitrophenylhydrazine; hydroxyl radical; protein carbonyl; peroxynitrite; hypochlorous acid; hemoglobin; myoglobin; cytochrome C; review;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Leeuwenburgh, C Univ Florida, Biochem Aging Lab, POB 118206, Gainesville, FL 32611 USA Univ Florida POB 118206 Gainesville FL USA 32611 32611 USA
Citazione:
S. Adams et al., "Reactive carbonyl formation by oxidative and non-oxidative pathways", FRONT BIOSC, 6, 2001, pp. A17-A24

Abstract

The spectrophotometric protein carbonyl assay is used as an indicator of protein damage by free radical reactions in vitro and in a variety of pathologies. We investigated model proteins and a variety of oxidative and non-oxidative reactions, as well as what effects hemoglobin, myoglobin, and cytochrome c might have on levels of protein carbonyls. We show that oxidative as well as non-oxidative mechanisms introduce carbonyl groups into proteins,providing a moiety for quantification with 2,4-dinitrophenylhydrazine (DNPH). Bovine serum albumin exposed to oxidative scenarios, such as hypochlorous acid, peroxynitrite, and metal-catalyzed oxidation exhibited variable, but increased levels of carbonyls. Other non-oxidative modification systems,in which proteins are incubated with various aldehydes, such as malondialdehyde, acrolein, glycolaldehyde, and glyoxal also generated significant amounts of carbonyls. Furthermore, purified myoglobin, hemoglobin, and cytochrome c show high absorbance at the same wavelengths as DNPH. The high levelsobserved are due to the innate absorbance of hemoglobin, myoglobin, and cytochrome c near the assay spectra of DNPH. These studies show that carbonylcontent could be due to oxidative as well as non-oxidative mechanisms and that heme-containing compounds may effect carbonyl quantification.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 06:56:15