Properties of the thermostable glutamate dehydrogenase of the mesophilic anaerobe Peptostreptoccus asaccharolyticus purified by a novel method after over-expression in an Escherichia coli host

FEMS Microbiology Letters

Volumn 244, Issue 1, 2005, Pages 53-59

  Carrigan, John B ^a   Coughlan, Suzie ^a,b   Engel, Paul C ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

^b National Virus Reference Laboratory   (Ireland)

Author keywords

Coenzyme specificity; Glutamate dehydrogenase; Overexpression; Peptostreptococcus; Purification; Thermophilicity; Thermostability

Indexed keywords

BACTERIAL ENZYME; GLUTAMATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ANAEROBIC BACTERIUM; ARTICLE; CONTROLLED STUDY; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; HEATING; NONHUMAN; PEPTOSTREPTOCOCCUS; PEPTOSTREPTOCOCCUS ASACCHAROLYTICUS; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

ESCHERICHIA COLI; PEPTONIPHILUS ASACCHAROLYTICUS; PEPTOSTREPTOCOCCUS;

EID: 13844307122     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2005.01.026     Document Type: Article

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