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Titolo:
Bathocuproine-assisted reduction of copper(II) by human albumin
Autore:
Ivanov, AI; Parkinson, JA; Cossins, E; Woodrow, J; Sadler, PJ;
Indirizzi:
Univ Edinburgh, Dept Chem, Edinburgh EH9 3JJ, Midlothian, Scotland Univ Edinburgh Edinburgh Midlothian Scotland EH9 3JJ Midlothian, Scotland Belarus Acad Sci, Inst Bioorgan Chem, Minsk 220141, Byelarus Belarus Acad Sci Minsk Byelarus 220141 rgan Chem, Minsk 220141, Byelarus Delta Biotechnol Ltd, Nottingham NG7 1FD, England Delta Biotechnol Ltd Nottingham England NG7 1FD tingham NG7 1FD, England
Titolo Testata:
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
fascicolo: 1, volume: 5, anno: 2000,
pagine: 102 - 109
SICI:
0949-8257(200002)5:1<102:BROCBH>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOW-DENSITY-LIPOPROTEIN; AMYLOID PRECURSOR PROTEIN; HUMAN-SERUM ALBUMIN; HYDROGEN-PEROXIDE; HYDROXYL RADICALS; L-HISTIDINE; OXIDATION; BINDING; SITE; DAMAGE;
Keywords:
bathocuproinedisulfonate; human albumin; copper; reduction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Sadler, PJ Univ Edinburgh, Dept Chem, W Mains Rd, Edinburgh EH9 3JJ, Midlothian, Scotland Univ Edinburgh W Mains Rd Edinburgh Midlothian Scotland EH93JJ
Citazione:
A.I. Ivanov et al., "Bathocuproine-assisted reduction of copper(II) by human albumin", J BIOL I CH, 5(1), 2000, pp. 102-109

Abstract

Human albumin (studied here as the recombinant protein rHA), a copper-binding protein in blood plasma. is shown to reduce Cu(II) to Cu(I) in the presence of a Cu(I) chelator, bathocuproinedisulfonate (BD). This reaction was accelerated at low pH, when there was little binding of Cu(II) to rHA, The addition of a competitive metal ion, Ni(II), or an increase in the concentration of ED, enhanced the reduction of Cu(II) to Cu(I). It was concluded that the oxidant was the Cu(II) complex of ED. which is likely to bind strongly to albumin. The free thiol at Cys34 was ruled out as the sole reducing agent, since Cys34-blocked albumin also gave rise to Cu(I) in the presence of ED. Reactions with amino acids and peptides suggested that Tyr and possibly His side-chains are potential reductants, ED and its homologues are frequently used as Cu(I)-specific chelators in biological experiments, but the strong oxidant activity of [Cu(II)(BD)(2)](2-) and its ability to bind to biological macromolecules should not be overlooked, and may artificially trigger/accelerate Cu(II) reduction.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 07:55:10