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oligomer
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in mitochondria from intact animals, mCK exists as a mixture of two oligomeric forms (dimer and octamer: 68 and 32%, respectively). Cerebral ischemia changes the dimer/octamer ratio. This ratio is shifted toward the formation of dimers after 30-min ischemia
polymer
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x * 47000, head mitochondrial isozyme, SDS-PAGE
?
x * 44000, His6-tagged enzyme, SDS-PAGE
?
x * 43000, His6-tagged enzyme, SDS-PAGE
?
x * 43264, calculated from amino acid sequence
?
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x * 40000-44000, mature enzyme
dimer
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dimer
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2 * 35000, SDS-PAGE
dimer
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2 * 40000, SDS-PAGE
dimer
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2 * 40000-44000, mature cytosolic isozymes
dimer
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2 * 41000, SDS-PAGE
dimer
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2 * 43000, recombinant enzyme, SDS-PAGE, dimer formation after dissociation of the octamer
dimer
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2 * 41000, muscle cytosolic isozyme, SDS-PAGE
dimer
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2 * 45000, SDS-PAGE, isoform CK2
dimer
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2 * 40000-43000, SDS-PAGE
dimer
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2 * 44000, SDS-PAGE, presence of 2-mercaptoethanol, high speed sedimentation equilibrium centrifugation of urea-treated enzyme
dimer
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2 * 42000, SDS-PAGE
dimer
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2 * 43000, SDS-PAGE
dimer
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2 * 41500, SDS-PAGE
dimer
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crystallization data, absence of ATP
dimer
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2 * 43195, calculated from sequence of cDNA
dimer
2 * 40000-44000, mature cytosolic isozymes
dimer
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2 * 41000, SDS-PAGE
dimer
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2 * 42000, SDS-PAGE
dimer
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2 * 43000, SDS-PAGE, but also octamer
dimer
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2 * 43600, SDS-PAGE, but also octamer, electron microscopy
dimer
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2 * 40000-44000, mature cytosolic isozymes
dimer
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2 * 50000, SDS-PAGE
dimer
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2 * 40000-44000, mature cytosolic isozymes
dimer
2 * 47000, about, recombinant wild-type enzyme and recombinant mutant enzymes D209A and R151A, SDS-PAGE
dimer
muscle creatine kinase is only enzymatically active as a dimer
dimer
dual active-site cysteine 283 residues, spectral observations localized at the active-site cysteines indicate an intrinsic, dynamic asymmetry between the two subunits that exists already in the apo form of the dimeric creatine kinase enzyme, rather than being induced by the substrate. Unmodified and Cys283-modified enzymes are investigated in the apo and transition state analogue forms of the enzyme. The narrow and invariant S-H vibrational bands report a homogeneous environment for the unmodified active-site cysteines, indicating that their thiols are hydrogen bonded to the same H-bond acceptor in the presence and absence of the substrate. The S-H peak persists at all physiologically relevant pH's, indicating that Cys283 is protonated at all pH's relevant to enzymatic activity. The S-H hydrogen bond acceptor is a single, long-resident water molecule and the role of the conserved yet catalytically unnecessary thiol may be to dynamically rigidify that part of the active site through specific H-bonding to water. The asymmetric and broad CN stretching bands from the CN-modified Cys283 suggest an asymmetric structure in the apo form of the enzyme in which there is a dynamic exchange between spectral subpopulations associated with water-exposed and water-excluded probe environments, homogeneous orientation of the SCN probe group in the active site. Molecular dynamics simulations, overview
dimer
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2 * 49000, SDS-PAGE
dimer
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2 * 43000-44000, SDS-PAGE, presence of 2-mercaptoethanol
dimer
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2 * 40000-43000, SDS-PAGE
dimer
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2 * 42000, isozyme CK-III
dimer
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2 * 41000, isozyme CK-IV
dimer
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1 * 41000 + 1 * 42000, isozyme CK-II
heterodimer
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heterodimer
1 * 47200 + 1 * 43600, calculated from amino acid sequence
homodimer
2 * 45000, SDS-PAGE
homodimer
2 * 42000, SDS-PAGE
homodimer
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2 * 43000, using NMR chemical-shift perturbation and relaxation experiments designed to study the active site 320s flexible loop of muscle creatine kinase it is shown that each subunit can bind substrates independently
monomer
1 * 47000, about, recombinant mutant enzymes D209A, R147A, and R147A/R151A, SDS-PAGE
monomer
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1 * 145000, flagellar isozyme, SDS-PAGE
octamer
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8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
octamer
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8 * 43000, recombinant enzyme, SDS-PAGE, enzyme primarily forms octamers
octamer
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8 * 43000, muscle mitochondrial isozyme, SDS-PAGE
octamer
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8 * 41000, SDS-PAGE, isoform CK1
octamer
mitochondrial isozyme MtCK
octamer
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crystallization data
octamer
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8 * 42000, SDS-PAGE, octameric structure dissociates during storage at -20°C, pH above 8.5, protein concentration below 0.3 mg/ml to dimeric form
octamer
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crystallization data, presence of ATP
octamer
8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
octamer
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8 * 43600, SDS-PAGE, but also dimer, electron microscopy
octamer
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8 * 43000, SDS-PAGE, also as dimer
octamer
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8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
octamer
mitochondrial isozyme
octamer
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8 * 40000-44000, mature mitochondrial isozymes, can dissociate to dimers dependent on conditions
octamer
mitochondrial isozyme
octamer
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mitochondrial isozyme
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additional information
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hydrolytic cleaveage is responsible for conversion of isoform MM1 to MM2 and MM3
additional information
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the octamer-dimer equilibrium highly depends on protein concentration and dilution, respectively, and on temperature, highest percentage of octamer occurs at 28°C, the lowest at 2°C, overview
additional information
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MtCK generally exists as an octamer, but a dynamic octamer/dimer equilibrium exists in vitro depending on various parameters like MtCK concentration, temperatures and pH. Enzyme activity and temperature stability /sensitivity are higher for the octameric enzyme than for the dimeric enzyme. MtCK dimers are very sensitive and inactivate after exposure to temperatures above 30°C
additional information
MtCK generally exists as an octamer, but a dynamic octamer/dimer equilibrium exists in vitro depending on various parameters like MtCK concentration, temperatures and pH. Enzyme activity and temperature stability /sensitivity are higher for the octameric enzyme than for the dimeric enzyme. MtCK dimers are very sensitive and inactivate after exposure to temperatures above 30°C
additional information
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overview on isoforms
additional information
Frog
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overview on isoforms
additional information
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overview on isoforms
additional information
analysis of the structure of cardiac sarcomeric mitochondrial isozyme, free or bound to MgATP or transition state analogue complex
additional information
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recurrent interaction of brain-type enzyme isoform with cis-Golgi matrix protein GM130. GM130 and creatine kinase co-localize specifically in a transient fashion during early prophase of mitosis, when GM130 plays an important role in Golgi apparatus fragmentation
additional information
formation of the disulfide bond between the C74 and the C146 residues in the oxidized form
additional information
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formation of the disulfide bond between the C74 and the C146 residues in the oxidized form
additional information
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overview on isoforms
additional information
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overview on isoforms
additional information
dimerization is no prerequisite for activity but is required for stability and quarternary structure, subunit interface structure and interacting side chains of Glu17, Tyr19, sp53, Gln57, Asp61, Asp209, Arg147, and Arg151, overview
additional information
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dimerization is no prerequisite for activity but is required for stability and quarternary structure, subunit interface structure and interacting side chains of Glu17, Tyr19, sp53, Gln57, Asp61, Asp209, Arg147, and Arg151, overview
additional information
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structure-function analysis, the monomeric enzyme is active, the subunits act independently
additional information
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the isozymes form monomers upon freeze-drying due to loss of subunit interactions
additional information
mutants L110D, L115D, L121D are faster on SDS-PAGE than wild-type protein
additional information
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mutants L110D, L115D, L121D are faster on SDS-PAGE than wild-type protein
additional information
study on adsorption of creatine kinase onto silicon wafers. At pH 4, enzyme monomers in solution adsorb, forming a very thin layer indicating creatine kinase unfolding. At pH 6.8, the adsorbed layer is composed of a mixture of enzyme dimers in native structure and film thickness is increased. At pH 9, creatine kinase dimers form monolayers with the higest thickness. In comparison to free enzyme in solution, adsorbed enzyme presents a shift of the optimal pH value from 6.8 toward alkaline pH
additional information
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tertiary structure of oxidized form of enzyme is more easily disturbed than reduced form. The oxidized form, unlike reduced form, cannot interact with the M-line protein myomesin and therefore might have no role in muscle contraction. Oxidized creatine kinase can be rapidly ubiquitinated by muscle ring finger protein I and may be substrate of the ATP-ubiquitin-proteasome pathway
additional information
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overview on isoforms