Construction, separation and properties of hybrid hexamers of glutamate dehydrogenase in which five of the six subunits are contributed by the catalytically inert D165S

European Journal of Biochemistry

Volumn 268, Issue 5, 2001, Pages 1173-1180

  Hayden, Bronagh M ^a   Engel, Paul C ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

Allosteric interaction; Glutamate dehydrogenase; Subunit hybrids

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); BETA CYCLODEXTRIN; CHAPERONE; GLUTAMATE DEHYDROGENASE; HYBRID PROTEIN; MUTANT PROTEIN; POLIDOCANOL; PROTEIN SUBUNIT;

ALLOSTERISM; ARTICLE; BINDING SITE; CLOSTRIDIUM; ENZYME ACTIVITY; ENZYME BINDING; ENZYME DENATURATION; ION EXCHANGE CHROMATOGRAPHY; KINETICS; MOLECULAR HYBRIDIZATION; PRIORITY JOURNAL; PROTEIN FOLDING; ULTRAFILTRATION;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; AMINO ACID SUBSTITUTION; CATALYSIS; CHROMATOGRAPHY, AFFINITY; CLOSTRIDIUM; COLORING AGENTS; CYSTEINE; DITHIONITROBENZOIC ACID; GLUTAMATE DEHYDROGENASE; GLUTAMIC ACID; HYDROGEN-ION CONCENTRATION; KINETICS; LIGANDS; MUTATION; NAD; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; RECOMBINANT FUSION PROTEINS; TRIAZINES; ULTRAFILTRATION; UREA;

CLOSTRIDIUM;

EID: 0035081796     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.01949.x     Document Type: Article

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