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Titolo:
PROPERTIES OF CATALYTIC SITE OF 28 KD PROTEIN (1-CYS PEROXIREDOXIN) FROM RAT OLFACTORY EPITHELIUM
Autore:
NOVOSELOV VI; PESHENKO IV; EVDOKIMOV VA; KAMZALOV SS; NOVOSELOV SV; NIKOLAEV YV; BYSTROVA MF; FESENKO EE;
Indirizzi:
RUSSIAN ACAD SCI,INST CELL BIOPHYS PUSHCHINO 142292 MOSCOW REGION RUSSIA
Titolo Testata:
Biofizika
fascicolo: 4, volume: 43, anno: 1998,
pagine: 610 - 616
SICI:
0006-3029(1998)43:4<610:POCSO2>2.0.ZU;2-7
Fonte:
ISI
Lingua:
RUS
Soggetto:
ALKYL HYDROPEROXIDE REDUCTASE; THIOL-SPECIFIC ANTIOXIDANT; PEROXIDE;
Keywords:
THIOL-SPECIFIC ANTIOXIDANTS; PEROXIREDOXINS; OLFACTORY EPITHELIUM; RAT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
15
Recensione:
Indirizzi per estratti:
Citazione:
V.I. Novoselov et al., "PROPERTIES OF CATALYTIC SITE OF 28 KD PROTEIN (1-CYS PEROXIREDOXIN) FROM RAT OLFACTORY EPITHELIUM", Biofizika, 43(4), 1998, pp. 610-616

Abstract

The secretory 28 kD protein, an abundant water-soluble protein from rat olfactory epithelium, belongs to the 1-Cys subfamily of thiol-specific antioxidants (peroxiredoxins). The 28 kD protein contains a singlecystein residue at; the position 46 which accounts for the antioxidant activity. Here we studied the effects of N-ethilmaleimide and t-butil hydroperoxide on the antioxidant: activity of the 28 kD protein and that of the 23 kD protein from rat erythrocyte which. is a member of 2-Cys subfamily of peroxiredoxines. N-ethilmaleimide, modificator for cystein residues, had no effect on antioxidant: activity of the dithiothreitol-treated 28 kD protein but irreversibly inhibited activity of the 23 kD protein under reducing conditions. The 28 kD protein was sensitive to treatment with peroxides: t-butyI hydroperoxide at micromolarconcentrations was shown to irreversibly inactivate 28 kD protein. Inthe presence of dithiothreitol, the lower level of peroxide concentrations was required to inhibit 28 kD protein activity. The mechanism ofthis effect may be mediated through conversion of sulfhydril group of46Cys to oxidazed states (46Cys-SO2N: and 46Cys-SO3H). Antioxidant property of 23 kD protein was impaired by t-butyl hydroperoxide only in the presence of dithiothreitol. The concentrations of t-butyl hydroperoxide needed to affect the 23 kD protein were at least one order of magnitude higher than were required for the 28 kD protein inhibition. The given results suggest the essential differences between catalytic site of 28 kD protein and that of 2-Cys peroxiredoxines.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 21:19:24