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Titolo:
Human dehydroepiandrosterone sulfotransferase: purification and characterization of a recombinant protein
Autore:
Chang, HJ; Zhou, M; Lin, SX;
Indirizzi:
CHU Laval, Res Ctr, MRC, Oncol Grp, St Foy, PQ G1V 4G2, Canada CHU Laval St Foy PQ Canada G1V 4G2 Oncol Grp, St Foy, PQ G1V 4G2, Canada CHU Laval, Res Ctr, Mol Endocrinol Lab, St Foy, PQ G1V 4G2, Canada CHU Laval St Foy PQ Canada G1V 4G2 crinol Lab, St Foy, PQ G1V 4G2, Canada Univ Laval, St Foy, PQ G1V 4G2, Canada Univ Laval St Foy PQ Canada G1V 4G2 niv Laval, St Foy, PQ G1V 4G2, Canada
Titolo Testata:
JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY
fascicolo: 2-3, volume: 77, anno: 2001,
pagine: 159 - 165
SICI:
0960-0760(200105)77:2-3<159:HDSPAC>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN CYTOSOLIC SULFOTRANSFERASES; HUMAN-LIVER; RAT-LIVER; HYDROXYSTEROID SULFOTRANSFERASE; STEROID SULFOTRANSFERASES; MOLECULAR-CLONING; IMMUNOLOGICAL CHARACTERIZATION; CDNA CLONING; HUMAN-FETUS; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Lin, SX CHU Laval, Res Ctr, MRC, Oncol Grp, 2705 Laurier Blvd, St Foy, PQ G1V 4G2,Canada CHU Laval 2705 Laurier Blvd St Foy PQ Canada G1V 4G2 1V 4G2,Canada
Citazione:
H.J. Chang et al., "Human dehydroepiandrosterone sulfotransferase: purification and characterization of a recombinant protein", J STEROID B, 77(2-3), 2001, pp. 159-165

Abstract

Dehydroepiandrosterone sulfate is the most abundant sulfated steroid transformed in human tissues and serves as a precursor for steroid hormones. Recombinant human dehydroepiandrosterone sulfotransferase (DHEA-ST) expressed in glutathione sulfotransferase fusion form in E. toll was purified using glutathione sepharose 4B affinity adsorption chromatography. a Factor Xa cleavage step, and Q-sepharose fast flow column chromatography. The homogeneous preparation had an activity toward dehydroepiandrosterone (DHEA) of 150 +/- 40 nmol/min per mg of protein under the assay conditions at an overall yield of 38.4% The recombinant human DHEA-ST was shown to have a subunit mass of 34 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. while having a molecular mass of 67.2 kDa by Superose-12 gel filtration. Ourresults indicate that the active recombinant enzyme expressed in E. coli is a homodimer. Biochemical properties for purified DHEA-ST were studied using DHEA as a substrate. The optimum pH ranged from pH 7 to 8, and the optimum temperature40-45 degreesC. Ninety percent of basal DHEA-ST activity remained even after the enzyme was treated at 45 degreesC for 15 min. The 50% inactivation concentration of NaCl for DHEA-ST activity was determined to be around 500 mM. The K-m value for DHEA was 1.9 +/- 0.3 muM and V-max = 190 +/- 18 nmol/min per mg of protein at 37 degreesC, pH 7.5. (C) 2001 Published by ElsevierScience Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 21:58:58