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Titolo:
Purification and stabilization of a monomeric isocitrate dehydrogenase from Corynebacterium glutamicum
Autore:
Bai, C; Fernandez, E; Yang, H; Chen, RD;
Indirizzi:
Univ Saskatchewan, Coll Med, Dept Biochem, Saskatoon, SK S7N 5E5, Canada Univ Saskatchewan Saskatoon SK Canada S7N 5E5 skatoon, SK S7N 5E5, Canada
Titolo Testata:
PROTEIN EXPRESSION AND PURIFICATION
fascicolo: 3, volume: 15, anno: 1999,
pagine: 344 - 348
SICI:
1046-5928(199904)15:3<344:PASOAM>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
COENZYME SPECIFICITY; ENZYME; BACTERIUM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
10
Recensione:
Indirizzi per estratti:
Indirizzo: Chen, RD UnivNSaskatchewan, Coll Med, Dept Biochem, 107 Wiggins Rd, Saskatoon, SK S7 Univ Saskatchewan 107 Wiggins Rd Saskatoon SK Canada S7N 5E5 K S7
Citazione:
C. Bai et al., "Purification and stabilization of a monomeric isocitrate dehydrogenase from Corynebacterium glutamicum", PROT EX PUR, 15(3), 1999, pp. 344-348

Abstract

Monomeric isocitrate dehydrogenase was expressed in Corynebacterium glutamicum cells harboring pEK-icdES1, a plasmid carrying the gene for the enzyme. Two- to three-fold higher expression levels of the recombinant enzyme were observed in such cells when grown in fermenters, compared to those grown in shaker incubators. The enzyme was purified to homogeneity by ammonium sulfate fractionation, Sephadex G-150 gel filtration, FPLC Mono Q anion-exchange chromatography, and affinity gel chromatography. Approximately 4 mg of 98% pure recombinant enzyme was obtained per liter of bacterial culture. Our results also include optimum buffer conditions for purification and storage of the enzyme. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 22:16:28