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Titolo:
PURIFICATION AND CHARACTERIZATION OF GLUTAREDOXIN (THIOLTRANSFERASE) FROM RICE (ORYZA-SATIVA L)
Autore:
SHA S; MINAKUCHI K; HIGAKI N; SATO K; OHTSUKI K; KURATA A; YOSHIKAWA H; KOTARU M; MASUMURA T; ICHIHARA K; TANAKA K;
Indirizzi:
KYOTO PREFECTURAL UNIV,DEPT BIOCHEM,COLL AGR KYOTO 606 JAPAN KYOTO PREFECTURAL UNIV,DEPT BIOCHEM,COLL AGR KYOTO 606 JAPAN JCR PHARMACEUT CO LTD,DEV & RES LABS,NISHI KU KOBE HYOGO 65122 JAPAN KYOTO PREFECTURAL UNIV,DEPT FOOD SCI & NUTR KYOTO 606 JAPAN KOKA WOMENS JR COLL,FAC HUMAN LIFE SCI,DEPT FOOD & NUTR,NISHIKYOGO KUKYOTO 615 JAPAN
Titolo Testata:
Journal of Biochemistry
fascicolo: 5, volume: 121, anno: 1997,
pagine: 842 - 848
SICI:
0021-924X(1997)121:5<842:PACOG(>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
PIG-LIVER THIOLTRANSFERASE; AMINO-ACID-SEQUENCE; GLUTATHIONE-DEPENDENT SYNTHESIS; ESCHERICHIA-COLI GLUTAREDOXIN; CALF THYMUS GLUTAREDOXIN; DEHYDROASCORBATE REDUCTASE; CYTOPLASMIC THIOLTRANSFERASE; RAT-LIVER; DISULFIDE OXIDOREDUCTASE; SPECTROPHOTOMETRIC ASSAY;
Keywords:
DEHYDROASCORBATE REDUCTASE ACTIVITY; GLUTAREDOXIN (THIOLTRANSFERASE); RICE BRAN; THIOL-DISULFIDE INTERCHANGE; THIOREDOXIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
57
Recensione:
Indirizzi per estratti:
Citazione:
S. Sha et al., "PURIFICATION AND CHARACTERIZATION OF GLUTAREDOXIN (THIOLTRANSFERASE) FROM RICE (ORYZA-SATIVA L)", Journal of Biochemistry, 121(5), 1997, pp. 842-848

Abstract

We purified and characterized glutaredoxin (thioltransferase), which catalyzes thiol/disulfide exchange reaction, for the first time in plants, The purification procedure employed an immunoabsorbent, antiglutaredoxin-Sepharose. Glutaredoxin was purified about 2,200-fold from rice bran and it appeared to be homogeneous on SDS-PAGE, MALDI-TOF mass spectrometry revealed that the protein has a molecular mass of 11,097.9Da. Rice glutaredoxin consists of 105 amino acid residues, containingthe tetrapeptide -Cys-Phe-Pro (Tyr)-Cys-, which constitutes the active site of Escherichia coli and mammalian glutaredoxins. Inactivation assay also indicated that cysteine residues are responsible for enzyme activity, Kinetic analyses revealed that the enzyme did not exhibit normal Michaelis-Menten kinetics, The enzyme has an optimum pH of about 8.7 with 2-hydroxyethyl disulfide as a substrate, In addition, rice glutaredoxin has dehydroascorbate reductase activity, like mammalian glutaredoxin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:28:01