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Titolo:
The ubiquitous 38 kDa contaminant in glutamic acid decarboxylase preparation from the cytosol of Pichia pastoris after immobilised metal ion affinitychromatography is an alcohol dehydrogenase
Autore:
Law, RHP; Robinson, HC; Rowley, MJ; Mackay, IR;
Indirizzi:
Monash Univ, Dept Biochem & Mol Biol, Clayton, Vic 3800, Australia Monash Univ Clayton Vic Australia 3800 Biol, Clayton, Vic 3800, Australia
Titolo Testata:
BIOTECHNOLOGY LETTERS
fascicolo: 9, volume: 23, anno: 2001,
pagine: 697 - 703
SICI:
0141-5492(200105)23:9<697:TU3KCI>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
SACCHAROMYCES-CEREVISIAE; MONOCLONAL-ANTIBODIES; METHYLOTROPHIC YEASTS; METHYL FORMATE; PURIFICATION; EXPRESSION; HEMIACETAL; SECRETION; STIPITIS; GENES;
Keywords:
alcohol dehydrogenase; glutamic acid decarboxylase; immobilised metal affinity chromatography; methyl formate; Pichia;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Law, RHP Monash Univ, Dept Biochem & Mol Biol, Clayton, Vic 3800, Australia Monash Univ Clayton Vic Australia 3800 yton, Vic 3800, Australia
Citazione:
R.H.P. Law et al., "The ubiquitous 38 kDa contaminant in glutamic acid decarboxylase preparation from the cytosol of Pichia pastoris after immobilised metal ion affinitychromatography is an alcohol dehydrogenase", BIOTECH LET, 23(9), 2001, pp. 697-703

Abstract

We expressed a recombinant human glutamic acid decarboxylase (rhGAD) tagged with a hexa-histidine sequence in the Pichia pastoris cytosol. When rhGADwas purified from cell lysates by immobilised metal affinity chromatography, a 38 kDa contaminant protein was evident. This ubiquitous 38 kDa proteinwas as a yeast alcohol dehydrogenase isozyme that can bind strongly to nickel. Strategies for its removal are discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 08:15:15