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x * 28000, His6-tagged enzyme, SDS-PAGE
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x * 28000, His6-tagged enzyme, SDS-PAGE
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x * 60000, recombinant catalytic alpha-subunit, SDS-PAGE
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x * 27800, calculated from amino acid sequence
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x * 27800, calculated from amino acid sequence
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x * 29000, Glc-DH-I and GlcDH-IWG3, SDS-PAGE
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x * 34000, GlcDH-II and GlcDH-IV, SDS-PAGE
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x * 36000, enzyme form GlcDH-II, SDS-PAGE
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x * 98000, Western blot analysis
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x * 39000, SDS-PAGE, x * 39970, calculated
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x * 39000, SDS-PAGE, x * 39970, calculated
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x * 41261, calculated from amino acid sequence
dimer
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2 * 90000, SDS-PAGE
dimer
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2 * 41000, SDS-PAGE
homodimer
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2 * 28048, calculated from amino acid sequence
homodimer
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2 * 28048, calculated from amino acid sequence
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homodimer
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2 * 89000, 791 amino acid residues
homodimer
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2 * 90000, deduced from genome sequence
homotetramer
4 * 30000, SDS-PAGE
homotetramer
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4 * 30000, SDS-PAGE
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homotetramer
4 * 30000, SDS-PAGE
homotetramer
4 * 28000, SDS-PAGE, 120000 kDa by gel filtration, calculated: 261 amino acid residues, 27.8 kDa
homotetramer
gel filtration, 4 * 28000
homotetramer
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4 * 30000, SDS-PAGE
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homotetramer
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4 * 28000, SDS-PAGE, 120000 kDa by gel filtration, calculated: 261 amino acid residues, 27.8 kDa
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homotetramer
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gel filtration, 4 * 28000
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homotetramer
4 * 30000, gel filtration
homotetramer
4 * 28200, gel filtration
homotetramer
a significant hydrogen bond network is formed between the residue R166 of subunit A and E148 of both subunits A and B in mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R. In the homotetramer structure of wild-type enzyme BmGDH, the same interactions occur between subunit C (R166) and subunit D (E148)
homotetramer
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a significant hydrogen bond network is formed between the residue R166 of subunit A and E148 of both subunits A and B in mutant enzyme Q252L/E170K/S100P/K166R/V72I/K137R. In the homotetramer structure of wild-type enzyme BmGDH, the same interactions occur between subunit C (R166) and subunit D (E148)
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homotetramer
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4 * 28200, gel filtration
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homotetramer
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4 * 30000, gel filtration
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monomer
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1 * 48000, strain 150-1, SDS-PAGE
monomer
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1 * 51000, strain 93-1, SDS-PAGE
monomer
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1 * 48000, strain 150-1, SDS-PAGE
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monomer
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1 * 51000, strain 93-1, SDS-PAGE
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monomer
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1 * 48000, strain 150-1, SDS-PAGE
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monomer
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1 * 51000, strain 93-1, SDS-PAGE
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tetramer
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2 * 45000, gel filtration of inactive monomeric enzyme
tetramer
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2 * 45000, gel filtration of inactive monomeric enzyme
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tetramer
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4 * 31500, SDS-PAGE
tetramer
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4 * 59000, SDS-PAGE
tetramer
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4 * 40000, SDS-PAGE
tetramer
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4 * 30000, SDS-PAGE
tetramer
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x-ray crystallography
tetramer
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4 * 30000, X-ray crystallography
tetramer
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gel filtration
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tetramer
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4 * 30000, X-ray crystallography
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tetramer
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4 * 33000, SDS-PAGE
tetramer
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4 * 33000, SDS-PAGE
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tetramer
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4 * 41000, recombinant enzyme, SDS-PAGE
tetramer
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4 * 41000, recombinant enzyme, SDS-PAGE
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tetramer
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4 * 58000, SDS-PAGE
tetramer
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4 * 38000, SDS-PAGE
additional information
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additional information
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additional information
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the enzyme is an active tetramer at pH 6.5. By shifting the pH to 9, the enzyme is completely and reversibly dissociated into four inactive protomers
additional information
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the enzyme is an active tetramer at pH 6.5. By shifting the pH to 9, the enzyme is completely and reversibly dissociated into four inactive protomers
additional information
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at very low ionic strength, the tetrameric state becomes unstable, even at pH 6.5
additional information
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monomers, dimers and tetramers participate in aggregation equilibria which are dependent on enzyme and NaCl concentration and on the pH value
additional information
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complete dissociation at pH 9 is possible only at NaCl and KH2PO4 concentrations below 20 mM
additional information
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reversible dissociation in to inactive monomers at alkaline pH