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heterodimer
-
1 * 17600+ 1 * 31500, SDS-PAGE
octamer
-
and dimer and tetramer, 8 * 27000, SDS-PAGE
?
-
x * 185000, Cu,Zn-SOD, SDS-PAGE
?
-
x * 185000, Cu,Zn-SOD, SDS-PAGE
-
?
x * 15835, mass spectrometry and dynamic light scattering
?
x * 38159, mass spectrometry and dynamic light scattering
?
-
x * 38159, mass spectrometry and dynamic light scattering
-
?
-
x * 15835, mass spectrometry and dynamic light scattering
-
?
-
x * 19250, Cu,Zn-SOD, SDS-PAGE
?
-
x * 19250, Cu,Zn-SOD, SDS-PAGE
-
?
-
x * 18000, Cu,Zn-SOD, SDS-PAGE
?
-
x * 18000, Cu,Zn-SOD, SDS-PAGE
-
?
-
x * 175000, Cu,Zn-SOD, SDS-PAGE
?
-
x * 175000, Cu,Zn-SOD, SDS-PAGE
-
?
-
x * 31000, native enzyme, SDS-PAGE
?
x * 22650, sequence calculation
?
-
x * 22650, sequence calculation
-
?
x *17000, recombinant SOD1, SDS-PAGE, x * 45000, recombinant SOD1-Lys7, SDS-PAGE
?
-
x *17000, recombinant SOD1, SDS-PAGE, x * 45000, recombinant SOD1-Lys7, SDS-PAGE
-
?
x * 24225, calculated, x * 24000, SDS-PAGE
?
-
x * 15841, sequence calculation
?
x * 25000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 25000, recombinant His-tagged enzyme, SDS-PAGE
-
?
x * 24000, about, sequence calculation
?
x * 22931, Fe-SOD, amino acid sequence determination
?
-
x * 22931, Fe-SOD, amino acid sequence determination
-
?
x * 15500, calculated, x * 16000, SDS-PAGE
?
x * 25400, calculated, x * 28000, SDS-PAGE
?
x * 17000, SDS-PAGE, x * 15704, MALDI-TOF
?
x * 18000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 24989, sequence calculation, MnSOD
?
-
x * 24989, sequence calculation, MnSOD
-
?
-
x * 15920, sequence calculation, x * 18000, SDS-PAGE
?
-
x * 22000, recombinant Mn-SOD, SDS-PAGE
?
-
x * 15132, sequence calculation
?
-
x * 30000-31000, isozyme 1, SDS-PAGE, x * 15000, isozyme 2, SDS-PAGE
?
x * 15700, about, cytoplasmic CuZn-SOD, sequence calculation
?
-
x * 15764-15809, Cu,Zn-SOD wild-type and mutant D90A, electrospray mass spectroscopy
?
-
x * 22000, amino acid sequence determination
?
-
x * 15800, MALDI-TOF-MS
?
-
x * 15764-15809, Cu,Zn-SOD wild-type and mutant D90A, electrospray mass spectroscopy
-
?
-
x * 22000, amino acid sequence determination
-
?
x * 15832, sequence calculation
?
x * 15882, Cu/Zn-SOD sequence calculation
?
-
x * 15882, Cu/Zn-SOD sequence calculation
-
?
x * 24800, about, sequence calculation
?
-
x * 25000, SDS-PAGE
-
?
-
x * 25000, SDS-PAGE
-
?
Megalodesulfovibrio gigas
-
x * 22000, Fe-SOD, SDS-PAGE
?
Megalodesulfovibrio gigas Fe-SOD
-
x * 22000, Fe-SOD, SDS-PAGE
-
?
x * 21000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 45000, SDS-PAGE of native protein, x * 34000-38000 and x * 29000-33000, SDS-PAGE of deglycosylated protein
?
x * 32000, recombinant His-tagged enzyme, SDS-PAGE, x * 30960, recombinant His-tagged enzyme, sequence calculation
?
-
x * 22500-29000, nectarin I: Mn-SOD, SDS-PAGE and mass spectroscopy
?
-
x * 25000, SDS-PAGE
-
?
-
detection of isoforms with 34500, 36000 and 50000 Da in non-denaturing gels
?
x * 106000, or x * 97000, SDS-PAGE, differently glycosylated protein forms
?
-
x * 25000, recombinant enzyme, SDS-PAGE
?
-
x * 22000, Fe-SOD, SDS-PAGE
?
-
x * 24000, SDS-PAGE
-
?
-
x * 25000, mitochondria, SDS-PAGE
?
-
x * 25000, mitochondria, SDS-PAGE
-
?
-
x * 22500-24000, Fe-SOD, SDS-PAGE
?
x * 24228, calculated from sequence
?
-
x * 22500-24000, Fe-SOD, SDS-PAGE
-
?
-
x * 24228, calculated from sequence
-
?
-
x * 16400, Cu,Zn-SOD, SDS-PAGE
?
-
x * 15800-16600 , two isozymes, sequence calculation, x * 18000, SDS-PAGE
?
-
x * 15800-16600 , two isozymes, sequence calculation, x * 18000, SDS-PAGE
-
?
-
x * 25000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 15320, SaCSD1, sequence calculation
?
-
x * 30000, about, sequence calculation, x * 25000, recombinant enzyme, SDS-PAGE
?
-
x * 17600 + x * 31500, SDS-PAGE
?
-
x * 32000, native enzyme, SDS-PAGE
?
Thermochaetoides thermophila
x * 23000, SDS-PAGE
?
Thermochaetoides thermophila
x * 17700, recombinant enzyme, SDS-PAGE
?
-
x * 25000, SDS-PAGE
-
?
x * 26000, recombinant enzyme mutants H29A and H171A, SDS-PAGE
dimer
-
2 * 21600, SDS-PAGE after denaturation in boiling SDS
dimer
-
2 * 21600, SDS-PAGE after denaturation in boiling SDS
-
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
dimer
Anas platyrhynchos domestica CuZn-SOD
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
-
dimer
-
2 * 18100, Fe-SOD, SDS-PAGE
dimer
-
2 * 18100, Fe-SOD, SDS-PAGE
-
dimer
-
2 * 15821, Cu,Zn-SOD, sequence calculation
dimer
-
2 * 15821, Cu,Zn-SOD, sequence calculation
-
dimer
-
2 * 20000, SDS-PAGE
dimer
-
2 * 16300, SDS-PAGE
dimer
-
2 * 16000, SDS-PAGE, isoenzyme B
dimer
-
2 * 16000, SDS-PAGE, isoenzyme B
-
dimer
-
2 * 20000, Fe-SOD, SDS-PAGE
dimer
-
2 * 20000, Fe-SOD, SDS-PAGE
-
dimer
-
2 * 22000, Mn-SOD, SDS-PAGE
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
dimer
-
2 * 22000, Mn-SOD, SDS-PAGE
-
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
-
dimer
-
2 * 16000, SDS-PAGE
dimer
-
2 * 18300, Mn-SOD, SDS-PAGE
dimer
-
2 * 18300, Mn-SOD, SDS-PAGE
-
dimer
-
2 * 16500, Cu,Zn-SOD-II, SDS-PAGE
dimer
2 * 17900, SDS-PAGE
dimer
-
2 * 23000, gel filtration, isoenzyme 2 and 3
dimer
-
2 * 23000, gel filtration, isoenzyme 2 and 3
-
dimer
2 * 23652, SOD1, sequence calculation
dimer
2 * 26000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 15000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 18000, SDS-PAGE
dimer
-
2 * 18000, SDS-PAGE
-
dimer
-
2 * 22900, Mn-SOD
dimer
-
2 * 21000, Fe-SOD
dimer
-
2 * 22900, Mn-SOD
-
dimer
-
2 * 21000, Fe-SOD
-
dimer
-
2 * 22900, Mn-SOD
-
dimer
-
2 * 21000, Fe-SOD
-
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
-
dimer
-
2 * 23500, Mn-SOD, SDS-PAGE
dimer
-
the homodimer contains an extended C-terminal tail comprising residues 193-213. Dimer interface and domain interface structure analysis: the shortest domain contacts involve residues Phe17, Leu52, Phe53, Tyr71, and Phe75 on one domain and Val145, Pro151, Val154, Tyr173, Phe177, His180, Cys189, Leu198, Ile205, and His210 on the other domain, and the dimer interface is stabilized by 10 hydrogen bonds and approximately 102 non-bonded contacts, involving 32 residues from both chains, overview
dimer
-
wild-type holo-enzyme
dimer
2 * 33000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 15912, mass spectrometry
dimer
-
2 * 15912, mass spectrometry
-
dimer
2 * 34589, sequence calculation, 2 * 35000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 34652, recombinant His-tagged enzyme, mass spectrometry, 2 * 53000, recombinant thioredoxin-fusion enzyme, SDS-PAGE
dimer
-
2 * 22000, SDS-PAGE
dimer
-
2 * 22000, SDS-PAGE
-
dimer
-
2 * 18500, Fe-SOD, SDS-PAGE
dimer
-
2 * 18500, Fe-SOD, SDS-PAGE
-
dimer
-
2 * 17500, Cu,Zn-SOD
dimer
-
2 * 17500, Cu,Zn-SOD
-
dimer
-
2 * 24000, SDS-PAGE
dimer
-
2 * 24000, SDS-PAGE
-
dimer
-
2 * 15000-20000, SDS-PAGE
dimer
-
2 * 23100, SDS-PAGE
dimer
-
2 * 23100, SDS-PAGE
-
dimer
-
2 * 16800, SDS-PAGE
dimer
-
2 * 16800, SDS-PAGE
-
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
-
dimer
-
2 * 25000, SDS-PAGE
dimer
-
2 * 25000, SDS-PAGE
-
dimer
-
2 * 23000, SDS-PAGE
dimer
-
2 * 23500, SDS-PAGE
dimer
-
2 * 23500, SDS-PAGE
-
dimer
-
2 * 22000, SDS-PAGE
dimer
-
2 * 20400, SOD-3, SDS-PAGE
dimer
-
2 * 16500, SOD-1, SDS-PAGE
dimer
-
2 * 15700, SDS-PAGE
dimer
-
2 * 19000, SDS-PAGE
dimer
-
2 * 19000, SDS-PAGE
-
dimer
2 * 21251, mass spectrometry, 2 * 22000, SDS-PAGE
dimer
-
2 * 21700, Mn-SOD, SDS-PAGE
dimer
-
2 * 21700, Mn-SOD, SDS-PAGE
-
dimer
-
2 * 19500, Fe-SOD, SDS-PAGE
dimer
-
2 * 19500, Fe-SOD, SDS-PAGE
-
dimer
-
2 * 20000, SDS-PAGE
dimer
Radix lethospermi
-
2 * 30500, SDS-PAGE, MS
dimer
-
2 * 17000, SDS-PAGE
dimer
-
2 * 17000, SDS-PAGE
-
dimer
-
2 * 17000, SDS-PAGE
-
dimer
-
2 * 23600, about, recombinant enzyme, sequence calcualtion, 2 * 25000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 23600, about, recombinant enzyme, sequence calcualtion, 2 * 25000, recombinant enzyme, SDS-PAGE
-
dimer
-
a noncovalently bound homodimer, primary structure
dimer
-
a noncovalently bound homodimer, primary structure
-
dimer
-
2 * 18300, Cu,Zn-SOD, SDS-PAGE
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
dimer
-
cytoplasmic enzyme
dimer
-
cytoplasmic enzyme
-
dimer
-
2 * 18300, Cu,Zn-SOD, SDS-PAGE
-
dimer
-
2 * 16000, Cu,Zn-SOD, SDS-PAGE
-
dimer
-
cytoplasmic enzyme
-
dimer
-
2 * 23000, Fe-/Mn-SOD, SDS-PAGE
dimer
-
2 * 23000, Fe-/Mn-SOD, SDS-PAGE
-
dimer
-
2 * 22500, Fe-SOD, SDS-PAGE
dimer
-
2 * 15100, isoenzyme II, SDS-PAGE
dimer
-
isoenzyme I, SDS-PAGE
dimer
-
2 * 18200, SDS-PAGE
dimer
-
2 * 22500, Fe-SOD, SDS-PAGE
-
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
-
dimer
-
2 * 19500, isozyme II, SDS-PAGE
dimer
-
2 * 18500, isozyme I, SDS-PAGE
dimer
2 * 24270, sequence calculation
dimer
2 * 22400, calculated from sequence
dimer
2 * 24270, calculated from sequence
dimer
-
2 * 24270, calculated from sequence
-
dimer
-
2 * 22400, calculated from sequence
-
dimer
2 * 16800, SDS-PAGE
dimer
-
2 * 23000, isozyme SODI, SDS-PAGE
dimer
-
and tetramer and octamer, 2 * 27000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
-
dimer
-
2 * 17000, SOD-2, SDS-PAGE
dimer
-
2 * 15900, SOD-4, SDS-PAGE
dimer
-
2 * 14500, SOD-1, SDS-PAGE
dimer
-
2 * 14500, SOD-1, SDS-PAGE
-
dimer
-
2 * 17000, SOD-2, SDS-PAGE
-
dimer
-
2 * 15900, SOD-4, SDS-PAGE
-
homodimer
2 * 25000, SDS-PAGE
homodimer
in solution, 2 * 24577, sequence calculation and gel filtration
homodimer
2 * 24600, calculated from sequence
homodimer
-
2 * 24600, calculated from sequence
-
homodimer
-
2 * 25000, SDS-PAGE
-
homodimer
2 * 15600, about, sequence calculation
homodimer
2 * 17500, His-tagged enzyme, SDS-PAGE, 2 * 15160, sequence calculation
homodimer
2 * 17500, about, sequence calculation, 2 * 18800, about, SDS-PAGE
homodimer
enzyme tertiary structural modeling, each monomer contains an eight-barrel chain with seven loops
homodimer
-
2 * 23500, SDS-PAGE, 2 * 22532, sequence calculation
homodimer
-
2 * 23500, SDS-PAGE, 2 * 22532, sequence calculation
-
homodimer
2 * 59000, SDS-PAGE, 2 * 50230, sequence calculation
homodimer
2 * 59000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
-
2 * 38000, recombinant chimera MnSOD-VHb, SDS-PAGE
homodimer
-
2 * 34034, sequence calculation and mass spectrometry
homodimer
-
2 * 34034, sequence calculation and mass spectrometry
-
homodimer
2 * 23000, SDS-PAGE, 2 * 22930, sequence calculation
homodimer
-
2 * 23000, SDS-PAGE, 2 * 22930, sequence calculation
-
homodimer
-
2 * 31079, sequence calculation
homodimer
2 * 24800, cytMnSOD
homodimer
2 * 18000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
2 * 23500, about, sequence calculation, 2 * 31000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
-
2 * 23500, about, sequence calculation, 2 * 31000, recombinant His-tagged enzyme, SDS-PAGE
-
homodimer
-
2 * 20000, native enzyme, SDS-PAGE
homodimer
2 * 42000, recombinant GST-tagged SeCuZnSOD, SDS-PAGE, 2 * 15800, untagged enzyme, SDS-PAGE
homodimer
-
2 * 30000, SDS-PAGE
homodimer
-
2 * 23000, SDS-PAGE
homodimer
2 * 27400, claculated, 2 * 29700, SDS-PAGE
homodimer
2 * 15960, sequence calculation, 2 * 17000, recombinant enzyme, SDS-PAGE
homotetramer
in crystals, 4 * 24577, sequence calculation and gel filtration
homotetramer
-
4 * 22000, Mn-SOD, SDS-PAGE
homotetramer
-
4 * 14000, SDS-PAGE
homotetramer
-
4 * 21192, MALDI-TOF, 4 * 23000, SDS-PAGE
homotetramer
-
4 * 21192, MALDI-TOF, 4 * 23000, SDS-PAGE
-
homotetramer
4 * 24000, mtMnSOD
homotetramer
-
4 * 24000, SDS-PAGE and gel filtration
homotetramer
-
4 * 24000, SDS-PAGE and gel filtration
-
monomer
1 * 17500, His-tagged enzyme, SDS-PAGE, 1 * 15160, sequence calculation
monomer
-
1 * 100000, Mn-SOD, reducing SDS-PAGE
monomer
-
1 * 100000, Mn-SOD, reducing SDS-PAGE
-
monomer
1 * 50230, sequence calculation, 1 * 59000, SDS-PAGE
monomer
1 * 33000, recombinant enzyme, SDS-PAGE
monomer
1 * 16385, sequence calculation, 1 * 16400, about, recombinant His6-and thioredoxin-tagged enzyme, mass spectrometry and SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE after treatment with urea and 2-mercaptoethanol
monomer
-
1 * 33000, SDS-PAGE after treatment with urea and 2-mercaptoethanol
-
monomer
-
1 * 66000, SODI, 1 * 22000, SODII, SDS-PAGE
monomer
-
1 * 15700, SDS-PAGE
monomer
1 * 21400, about, sequence calculation, 1 * 27000, recombinant His-tagged enzyme, SDS-PAGE
monomer
-
crystallization data
monomer
1 * 21000, recombinant SodB, SDS-PAGE
monomer
-
1 * 21000, recombinant SodB, SDS-PAGE
-
monomer or dimer
-
the kinetic mechanism for holo SODs involves native dimer-monomer intermediate, and unfolded monomer, with variable metal dissociation from the monomeric states depending on solution conditions, overview. Naturally occuring mutants seem to favour increased formation of a Zn-free monomer intermediate, which is implicated in the formation of toxic aggregates. Kinetic basis for the extremely high stability of wild-type holo SOD, overview
monomer or dimer
x * 26000, SDS-PAGE
tetramer
4 * 23954, sequence calculation
tetramer
-
4 * 22340, Mn-SOD, sequence calculation
tetramer
-
4 * 22340, Mn-SOD, sequence calculation
-
tetramer
4 * 25400, Mn-SOD, SDS-PAGE
tetramer
4 * 27000, peroxisomal Mn-SOD, SDS-PAGE
tetramer
-
4 * 21300, SDS-PAGE
tetramer
-
4 * 28000, recombinant EC-SOD, SDS-PAGE
tetramer
-
4 * 21300, SDS-PAGE
-
tetramer
-
4 * 26000, Fe-SOD, SDS-PAGE
tetramer
-
4 * 26000, Fe-SOD, SDS-PAGE
-
tetramer
-
4 * 24096, amino acid sequence determination
tetramer
-
4 * 22321, MALDI-TOF, 4 * 24000-25000, SDS-PAGE in absence, 4 * 25000, in presence of 2-mercaptoethanol
tetramer
-
4 * 25000, SDS-PAGE
tetramer
-
4 * 25000, SDS-PAGE
-
tetramer
-
4 * 27000, Mn-SOD, SDS-PAGE
tetramer
-
4 * 27000, Mn-SOD, SDS-PAGE
-
tetramer
4 * 24000, SDS-PAGE
tetramer
4 * 24204, calculated from sequence
tetramer
-
4 * 24000, SDS-PAGE
-
tetramer
-
4 * 24204, calculated from sequence
-
tetramer
-
4 * 22400, Mn-SOD, SDS-PAGE
tetramer
-
4 * 22000, Mn-SOD, SDS-PAGE
tetramer
-
4 * 22000, Mn-SOD, SDS-PAGE
-
tetramer
-
4 * 22000, Mn-SOD, SDS-PAGE
-
tetramer
-
4 * 22400, Mn-SOD, SDS-PAGE
-
tetramer
-
4 * 24000, alpha2beta2, SDS-PAGE
tetramer
4 * 24000, recombinant enzyme, SDS-PAGE
tetramer
-
4 * 24000, wild-type and mutant enzymes, SDS-PAGE
tetramer
-
4 * 25000, Mn-SOD, reducing SDS-PAGE
tetramer
-
mitochondrial enzyme
tetramer
-
mitochondrial enzyme
-
tetramer
-
mitochondrial enzyme
-
tetramer
-
4 * 25000, Mn-SOD, reducing SDS-PAGE
-
tetramer
2 * 22400, simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a tetrameric form of the enzyme with a specific activity of about 2.5 times higher than the activity of the dimer, suggesting that even though the protein is stable and active in a dimeric state, its physiological form may be tetrameric
tetramer
-
2 * 22400, simultaneous treatment with low SDS concentrations and heat results in an almost quantitative conversion into a tetrameric form of the enzyme with a specific activity of about 2.5 times higher than the activity of the dimer, suggesting that even though the protein is stable and active in a dimeric state, its physiological form may be tetrameric
-
tetramer
4 * 21700, SDS-PAGE
tetramer
Thermochaetoides thermophila
-
4 * 23500, SDS-PAGE
tetramer
Thermochaetoides thermophila CT2
-
4 * 23500, SDS-PAGE
-
tetramer
-
4 * 22400, SDS-PAGE
tetramer
-
4 * 22400, SDS-PAGE
-
tetramer
-
4 * 21000, Mn-SOD, SDS-PAGE
tetramer
-
4 * 21000, Mn-SOD, SDS-PAGE
-
tetramer
-
4 * 21000, Mn-SOD, SDS-PAGE
tetramer
-
4 * 21000, Mn-SOD, SDS-PAGE
-
tetramer
-
4 * 21000, Mn-SOD, SDS-PAGE
-
tetramer
-
and dimer and octamer, 4 * 27000, SDS-PAGE
tetramer
4 * 23000, recombinant SodA, SDS-PAGE
tetramer
-
4 * 23000, recombinant SodA, SDS-PAGE
-
tetramer
-
4 * 24000, SOD-III, SDS-PAGE
tetramer
-
4 * 24000, SOD-III, SDS-PAGE
-
trimer or tetramer
-
x * 24140, mass spectrometry
trimer or tetramer
-
x * 24140, mass spectrometry
-
additional information
three-dimensional structure modelling, overview
additional information
-
three-dimensional structure modelling, overview
additional information
enzyme structural analysis by circular dichroism analysis, recombinnat AhSOD is an intrinsically disorder enzyme, sequence comparisons and three-dimensional model
additional information
-
enzyme structural analysis by circular dichroism analysis, recombinnat AhSOD is an intrinsically disorder enzyme, sequence comparisons and three-dimensional model
additional information
-
peptide mapping by tryptic digest and amino acid sequence determination and analysis, the enzyme does neither contain a Tyr residue nor a carbohydrate chain occupying an N-linkage site -N-I-Y-,overview, homology modeling of Cu/Zn-SOD
additional information
-
peptide mapping by tryptic digest and amino acid sequence determination and analysis, the enzyme does neither contain a Tyr residue nor a carbohydrate chain occupying an N-linkage site -N-I-Y-,overview, homology modeling of Cu/Zn-SOD
-
additional information
-
isoform SOD1 stabilizes and activates calcineurin in rat brain cytosol via a nearly 90fold decrease in the KM for p-nitrophenylphosphate. SOD1 prevents the loss of iron and Zn from the active site of calcineurin, possibly by a conformation-dependent interaction. SOD1 also activates human calcineurin by 74%
additional information
the enzyme exists in both monomeric and dimeric forms, the latter being more active. Circular dichroic spectroscopy analysis confirms the thermostable nature of Cj-Cu,Zn SOD, secondary structure analysis, overview
additional information
homology structure modeling of PgCuZnSOD, overview
additional information
-
homology structure modeling of PgCuZnSOD, overview
additional information
Cu,Zn-SOD exists as 70% dimeric form and 30% monomeric form
additional information
-
Cu,Zn-SOD exists as 70% dimeric form and 30% monomeric form
additional information
-
Cu,Zn-SOD exists as 70% dimeric form and 30% monomeric form
-
additional information
SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal
additional information
SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal
additional information
SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal
additional information
-
SOD1 possesses a short amino-terminal extension which could represent, in this heterotrophic dinoflagellate lacking a chloroplast, a putative mitochondrial targeting signal
additional information
MnSOD molecular modelling of the highly conserved sequence, structure modelling and comparison with MnSODs from other organisms
additional information
-
MnSOD molecular modelling of the highly conserved sequence, structure modelling and comparison with MnSODs from other organisms
additional information
-
MnSOD molecular modelling of the highly conserved sequence, structure modelling and comparison with MnSODs from other organisms
-
additional information
-
N-terminal amino acid sequence
additional information
modelling of the three-dimensional structure of SOD monomer, overview
additional information
-
three-dimensional structure of Mn-SOD monomer
additional information
-
three-dimensional structure of Mn-SOD monomer
-
additional information
-
isoform SOD1 stabilizes and activates calcineurin in rat brain cytosol by 47%
additional information
asymmetric structure of the zinc-deficient enzyme, overview
additional information
-
asymmetric structure of the zinc-deficient enzyme, overview
additional information
hEC-SOD is present both as a monomer (33 kDa) and a dimer (66 kDa), enzyme secondary structure determination by circular dichroism, recombinant hEC-SOD purified from Sf9 insect cells is mainly composed of beta-sheet structures
additional information
-
hEC-SOD is present both as a monomer (33 kDa) and a dimer (66 kDa), enzyme secondary structure determination by circular dichroism, recombinant hEC-SOD purified from Sf9 insect cells is mainly composed of beta-sheet structures
additional information
-
enzyme is only active as tetramer or pentamer
additional information
the enzyme sequence comprises eight beta-sheets forming a beta-barrel topology, alignment and modeling studies confirmed the conservation of Cu/ZnSOD at primary and tertiary levels. Structure homology modeling and three-dimensional structure, overview
additional information
-
the enzyme sequence comprises eight beta-sheets forming a beta-barrel topology, alignment and modeling studies confirmed the conservation of Cu/ZnSOD at primary and tertiary levels. Structure homology modeling and three-dimensional structure, overview
additional information
cytMnSOD is composed of a leader sequence with 61 amino acid peptide, putative Mn binding sites H111, H159, D244 and H248, two N-glycosylation sites, NHT and NMA, and the MnSOD domain, MSD. mtMnSOD is composed of putative Mn binding sites H49, H97, D181 and H185, two N-glycosylation sites, NHT and NLS, MSD, and a mitochondrial-targeting sequence with 21 aa peptide
additional information
cytMnSOD is composed of a leader sequence with 61 amino acid peptide, putative Mn binding sites H111, H159, D244 and H248, two N-glycosylation sites, NHT and NMA, and the MnSOD domain, MSD. mtMnSOD is composed of putative Mn binding sites H49, H97, D181 and H185, two N-glycosylation sites, NHT and NLS, MSD, and a mitochondrial-targeting sequence with 21 aa peptide
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cytMnSOD is composed of a leader sequence with 61 amino acid peptide, putative Mn binding sites H111, H159, D244 and H248, two N-glycosylation sites, NHT and NMA, and the MnSOD domain, MSD. mtMnSOD is composed of putative Mn binding sites H49, H97, D181 and H185, two N-glycosylation sites, NHT and NLS, MSD, and a mitochondrial-targeting sequence with 21 aa peptide
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amino-terminal peptide sequence
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the purified SOD appears to be monomeric and converts to its dimeric form with increased enzymatic activity in betel nut oral extract. This irreversible conversion is mainly induced by slaked lime, resulting from the increase in pH of the oral cavity. Oral extract from chewing areca nut alone also induces SOD dimerization due to the presence of arginine
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circular dichroism spectral analysis of the enzyme's secondary structure. The enzyme conserves the beta-barrel structure of the CuZn-SODs in its recombinant form
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circular dichroism spectral analysis of the enzyme's secondary structure. The enzyme conserves the beta-barrel structure of the CuZn-SODs in its recombinant form
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immunoblot analysis shows isoforms of 25 and 75 kDa with increased expression of the 75 kDa isoform after treatment with corticotrophin
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the N-terminal sequence of the purified native enzyme is VLKAVCVLKGTGEVT
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secondary, quarternary and three-dimensional structure
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secondary, quarternary and three-dimensional structure
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Thermochaetoides thermophila
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the enzyme contains the sequence TLPDLKYD at the N-terminus
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Thermochaetoides thermophila
subunit interface structure, overview
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Thermochaetoides thermophila CT2
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the enzyme contains the sequence TLPDLKYD at the N-terminus
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secondary structure analysis by CD spectroscopy, the enzyme has a high alpha-helical content of 70%, overview
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structure models of three enzyme mutants His29Ala, His84Ala, and His171Ala, overview
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secondary structure analysis by CD spectroscopy, the enzyme has a high alpha-helical content of 70%, overview
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amino acid sequence comparisons, the swortfish SOD has a higher content of arginine and tyrosine than the corresponding bovine enzyme and appears to dissociate more readily into subunits. The swortfish enzyme has a higher content of arginine and tyrosine, high homology with the other eukaryotic enzymes,and low homology with the Photobacterium leiognuthi enzyme
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secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodA contains 29% alpha-helix and 16% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
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secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodA contains 29% alpha-helix and 16% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
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secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodA contains 29% alpha-helix and 16% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
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secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodA contains 29% alpha-helix and 16% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
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secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodB contains 44% alpha-helix and 13% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
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secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodB contains 44% alpha-helix and 13% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
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secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodB contains 44% alpha-helix and 13% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
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secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodB contains 44% alpha-helix and 13% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
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secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodA contains 29% alpha-helix and 16% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
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secondary structure analysis using circular dichroism, overview. At pH 7.0 and 28°C, SodB contains 44% alpha-helix and 13% beta-sheets. The elements of secondary structures are more sensitive to pH than to temperature
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