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Titolo:
Purification and characterization of superoxide dismutase from chicken liver
Autore:
Ozturk-Urek, R; Tarhan, L;
Indirizzi:
Dokuz Eylul Univ, Fac Art & Sci, Dept Chem, TR-35150 Izmir, Turkey Dokuz Eylul Univ Izmir Turkey TR-35150 Dept Chem, TR-35150 Izmir, Turkey
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
fascicolo: 2, volume: 128, anno: 2001,
pagine: 205 - 212
SICI:
1096-4959(200102)128:2<205:PACOSD>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
COPPER; ENZYME;
Keywords:
superoxide dismutase; metaloenzyme; chicken liver; purification; pH activity; pH stability; thermal stability; inhibition effect; ionic strength activity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Tarhan, L Dokuz Eylul Univ, Fac Art & Sci, Dept Chem, TR-35150 Izmir, Turkey Dokuz Eylul Univ Izmir Turkey TR-35150 TR-35150 Izmir, Turkey
Citazione:
R. Ozturk-Urek e L. Tarhan, "Purification and characterization of superoxide dismutase from chicken liver", COMP BIOC B, 128(2), 2001, pp. 205-212

Abstract

Superoxide dismutase (SOD; EC 1.15.1.1) is an enzyme that protects againstoxidative stress from superoxide radicals in living cells. This enzyme hasbeen isolated, purified and partially characterized from chicken liver. The following steps were carried out in order to purify chicken liver SOD. Initially, the liver was homogenized and hemoglobin was removed. Subsequentlyprotein precipitation was effected with (NH4)(2)SO4, methanol, (NH4)(2)SO4-methanol and polyethylene glycol methods. The product from polyethylene glycol-3350 precipitation was found to have the highest SOD activity. Polyethylene glycol was removed by chromatography using a PD-10 column. After passing through an ultrafilter, the superoxide dismutase was fractionated by DEAE-ion chromatography and then Sephadex G-75 gel filtration chromatography. During this purification procedure, a specific activity of 4818.2 IU/mg was reached, corresponding to 285.8-fold purification. The purified enzyme, which was characterized as cyanide-sensitive SOD, contained two subunits having Cu and Zn elements with a molecular weight of 16000 +/- 500 for each. The optimum pH of purified CuZnSOD was determined to be 8.9. The enzyme was found to have good pH stability in the pH range 6.0-7.5 at 25 degreesC overa 2-h incubation period and displayed good thermal stability up to 45 degreesC at pH 7.4 over a 1-h incubation period. The SOD enzyme was not inhibited by DTT and beta -mercaptoethanol, but inhibited by CN- and H2O2. In the presence of 2 mM iodoacetamide, the enzyme showed an approximately 40% activity loss. Finally, the inhibitory effect of ionic strength on SOD was alsoinvestigated. (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 20:50:47