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2-(2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
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2-(2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
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2-(2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-yl)isoindoline-1,3-dione
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2-(3-(trifluoromethyl)phenyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
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2-(4-amidinophenyl)-6-indolecarbamidine
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significantly inhibits DNase I activity
2-(4-nitrobenzyl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
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2-(pyridin-2-yl)-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
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2-benzyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
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2-ethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
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2-Nitro-5-thiocyanobenzoic acid
2-nitro-5-thiosulfobenzoic acid
5'-deoxy-GMP
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competitive, product inhibition
Aflatoxin B2a
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non-competitive inhibitor
Aflatoxin G2
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non-competitive inhibitor
Aflatoxin G2a
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non-competitive inhibitor
Aflatoxin M1
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non-competitive inhibitor
Aprotinin
inhibits DNase1 as a result of plasmin inhibition
aurintricarboxylic acid
i.e ATA, a general inhibitor of nucleases, weak inhibition
Bile acids
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inhibit the enzyme in concert with cholesterol sulfate
calf spleen inhibitor protein II
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molecular weight: 59000 Da, forms an inhibitory uni-uni molecular complex with DNase I, maximum stability at pH 7
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calf thymus inhibitor protein
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molecular weight: 49000 Da, maximum stability at pH 6
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carbodiimide
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presence of divalent cations slows the rate of inactivation
Cholesterol sulfate
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from human gastric fluid, the sulfate group and the hydrophobic side chain of cholesterol sulfate are indispensable for the inhibitory effect, irreversible, dependent on bile acids, a ratio of 342:1 of bile acids to cholesterol sulfate is required for complete inhibition
Cu-iodoacetate
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at 0.1 M iodoacetate and 4 mM Cu2+ 50% inhibition in 16 min
DTT
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80% inhibition at 1 mM
E2-immunity protein
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complete inhibition of activity on plasmid DNA
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guanidinium hydrochloride
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over 80% inhibition at 0.5 M
K+
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no inhibition at 50 mM, 50% inhibition at 200 mM
methanesulfonylchloride
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inactivation at pH 5.0
Na+
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no inhibition at 50 mM, 50% inhibition at 200 mM
oligonucleotides
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competitive inhibition
plasmin
directly inhibits recombinant DNase1/3, but does not inactivate recombinant DNase1
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protein Im9
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an Escherichia coli protein that binds to E9 DNase in the cytosol to protect the cell
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RNA
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enhanced activity by pretreatment with ribonuclease, variety of RNA's including tRNA
Somatostatin
2 enzyme forms: a somatostatin-sensitive and a somatostatin-resistant, controls the enzyme level in the lower gut, in vivo transient down-regulation of gene expression of the sensitive enzyme form
Tris
increasing concentrations of Tris (approximately half activity in the presence of 80 mM Tris) have a greater inhibitory influence on rmDNase1/3 than on rmDNase1 (no inhibitory influence of Tris)
Urea
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20% inhibition at 4 M
2-mercaptoethanol
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70% inhibition at 1 mM
2-mercaptoethanol
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inactivation, reversal by the addition of 4 mM CaCl2, no inactivation if CaCl2 is present during the reducing reaction
2-mercaptoethanol
slight inhibition
2-mercaptoethanol
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inhibition after treatment with EGTA
2-mercaptoethanol
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inhibition, but reversal by addition of 3 mM CaCl2
2-Nitro-5-thiocyanobenzoic acid
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inhibition at identical rates
2-Nitro-5-thiocyanobenzoic acid
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inactivation by cleavage of peptide chain at positions 14, 40, 72 and 135
2-Nitro-5-thiocyanobenzoic acid
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inhibition at identical rates
2-nitro-5-thiosulfobenzoic acid
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the presence of Ca2+ or Mg2+ at pH 7.5 results in 80% inactivation without fragmentation of the enzyme. In the absence of metal ions it retains 80% of its activity. It binds DNase I through covalent modification, since dialysis and gel filtration can not reverse the inactivation reaction. After dilution into an acid buffer of pH 4.7, the inactivated enzyme regains about 40% of its initial activity. The inhibitor fails to inactivate other enzymes, suggesting that the inhibition is unique to DNase I
2-nitro-5-thiosulfobenzoic acid
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is a novel inhibitor specific for DNase I
actin
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inhibition of DNase I activity by increasing concentrations of actin dimer. At equimolar actin subunit to DNase I concentration its DNA degrading is inhibited to only about 50%, whereas full inhibition is obtained when the dimer concentration is that of DNase I, i.e., at double monomer concentration, suggesting that only one monomer of the actin dimer is able to inhibit the DNase I activity, although both appear to be able to bind DNase I. Gelsolin segment 1 bound to the dimer inhibits DNase I more effectively than uncomplexed dimer and has a higher affinity to DNase I than dimer alone
actin
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40 mM HEPES pH 7.0, 5 mM MgCl2, 1 mM CaCl2
actin
inhibits the DNA-nicking activity of DNAse I/CdtB chimera
actin
inhibition of enzyme by actin may serve as a self-protection mechanism against premature DNA degradtion during cell damage
Ca2+
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inhibitory above 1 mM
Ca2+
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slight inhibition of mutant D201A
Ca2+
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80% inhibition at 0.1 mM
Ca2+
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complete inhibition at 1-10 mM
Cu2+
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complete inhibition at 1-10 mM
Cu2+
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complete inhibition
EDTA
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EDTA
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current peaks of the Fc-oligo-SH-immobilized electrode are relatively stable within error before and after treatment of DNase I solution with EDTA or RNaseA solution, suggesting that this electrode can be used for the detection of DNase I activity specifically
EDTA
complete inhibition at 20 mM
EDTA
complete inhibition at 20 mM
EDTA
10 mM, complete loss of activity
EDTA
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50% inhibition at 0.3 mM
EDTA
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complete inhibition at 1 mM
EDTA
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inhibition observed above 50 microM, complete inhibition at 0.5 mM
EDTA
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complete ihibition at 1 mM; complete inhibition at 1 mM
EDTA
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complete inhibition at 10 mM
EDTA
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complete inhibition at 5 mM
EDTA
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complete inhibition at 1 mM
EGTA
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inhibition at 0.01 mM in the presence of 2.5 mM Mg2+
EGTA
complete inhibition at 5 mM
EGTA
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activity inhibited
EGTA
1 mM, complete loss of activity
EGTA
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inhibition at 1 mM
EGTA
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activity inhibited
EGTA
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complete inhibition at 1 mM
EGTA
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activity inhibited
EGTA
complete inhibition of the enzyme from serum at 5 mM
EGTA
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complete ihibition at 1 mM; complete inhibition at 1 mM
EGTA
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complete inhibition at 10 mM
EGTA
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complete inhibition at 1 mM
G-actin
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-
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G-actin
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DNase I causes depolymerization of F-actin to form a stable complex of 1 mol DNase I with 1 mol G-actin, this complex inhibits DNase I activity
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G-actin
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complete inhibition at 0.05 mg/ml
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G-actin
slight inhibition
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G-actin
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50% inhibition at 0.002 mg/ml
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G-actin
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15% inactivation at 0.004 mg
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G-actin
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complete inhibition at 0.001 mg
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G-actin
specific, strong inhibition
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G-actin
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heat labile inhibitor of DNase 1, released from white blood cells and platelets. Binds to and almost completely inhibits the nucleolytic activity of DNase 1. Inhibition of DNase 1 by actin (about 95% inhibition at equimolar ratio) requires ATP and leads both to the inhibition of DNase 1 and the depolymerization of the actin
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G-actin
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inhibition with actin-gelsolin segment I complex
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G-actin
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66% inhibition in an 1:1 molar ratio of DNase I-actin complex
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gamma-actin
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-
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heparin
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directly inhibits recombinant DNase1/3
heparin
directly inhibits recombinant DNase1/3
Hg2+
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iodoacetate
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inhibition in the presence of Mn2+ or Ca2+ at pH 7.2
iodoacetate
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formation of a 3-carboxymethyl histidine per molecule, in the presence of 0.1 M Mn2+ gradual inactivation
iodoacetate
strong inhibition in presence of Cu2+
iodoacetate
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complete inhibition
iodoacetate
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50% inhibition at 0.1 M in presence of 4 mM CuCl2 after 15 min
iodoacetate
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complete inhibition
KCl
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stimulating between 25 and 50 mM, inhibitory above 50 mM
KCl
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less inhibitory than NaCl
mannitol
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inhibition of enzyme activity during the entire growth period of seedlings
mannitol
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induces reduction in height and dry weight in seedlings due to increased enzyme activity in the initial growth stages followed by a decrease in subsequent days
N-bromosuccinimide
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inactivation by modification at Trp155
N-bromosuccinimide
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modification of Trp19, Trp155 and Trp 178, Trp155 most cruical for activity
NaCl
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stimulating between 25 and 50 mM, inhibitory above 50 mM
NaCl
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Na-DNA is inhibitory
NaCl
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inhibitory at concentrations below 100 mM
NaCl
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10fold lower activity at 150 mM
NaCl
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50% inhibition at 60 mM, mutated enzyme less sensitive against increased salt concentrations
NaCl
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decreasing activity with increasing ionic strength
NaCl
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50% inhibition at 80 mM and pH 5.8 and at 165 mM and pH 7.0
NaCl
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inhibitory at concentrations above 80 mM
NaCl
increasing concentrations of NaCl (approximately half activity in the presence of 50 mM NaCl) have a greater inhibitory influence on rmDNase1/3 than on rmDNase1 (approximately half activity in the presence of 150 mM NaCl)
phosphate
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SDS
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over 80% inhibition at 0.04% w/v
Tris-HCl buffer
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Tris-HCl buffer
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inhibition at high concentration
Trypsin
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is less resistant to trypsin than human DNase I, DNase I activity decreases gradually
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Trypsin
is less resistant to trypsin than human DNase I, DNase I activity decreases gradually
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Zn2+
-
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Zn2+
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complete inhibition at 1 mM
Zn2+
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complete inhibition at 1-10 mM
Zn2+
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inhibition at millimolar concentrations
Zn2+
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complete inhibition
additional information
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the phosphate residue is responsible for the inhibitory effect of guanosine 5'-nucleotides
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additional information
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no inhibition by sulfatides and membrane lipids, galactose ceramide, no inhibition by steroid sulfates such as estrone sulfate, pregnenolone sulfate, dehydroepiandrosterone sulfate, no inhibition by DMSO, Tween 20, sodium cholate, and sodium taurocholate
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additional information
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thermal stress substantially perturbs the secondary structure of DNase I. Accordingly, heating of solid DNase I samples to temperatures below or above the apparent denaturation temperatures of the solid protein degrades and hence denatures the protein. For denatured DNase I samples, the residual biological activities after heating to 125°C are 37% and the activities after heating to 210°C are ca. 8%. Thermal denaturation of DNase I in high sensitivity differential scanning calorimetry is not reversible upon cooling of thermally denatured proteins (in contrast to lysozyme). Lyophilised lysozyme better refolds than spray-dried DNase I
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additional information
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DTNB or Na2SO3 alone do not inactivate DNase I, even in the presence of divalent cations
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additional information
no inhibition by G-actin
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additional information
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no inhibition by G-actin; no inhibition by G-actin
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additional information
no inhibition by G-actin; no inhibition by G-actin
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additional information
resistant to trypsin inactivation in absence of Ca2+
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additional information
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resistant to trypsin inactivation in absence of Ca2+
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additional information
is resistant to trypsin
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additional information
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is resistant to trypsin
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additional information
G-actin has no effect on the ability of CdtB/DNAse I chimera to convert supercoiled DNA to relaxed and linear forms
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additional information
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G-actin has no effect on the ability of CdtB/DNAse I chimera to convert supercoiled DNA to relaxed and linear forms
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additional information
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efficiency of cleavage of DNA duplex on gold nanoparticles by DNase I is about 82% whereas the cleavage efficiency in solution phase at the same conditions is nearly 100%. Cleavage efficiencies using Pb2+-mediated DNA enzyme on gold nanoparticles and in solution phase are about 55% and 95%, respectively
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additional information
no inhibition by G-actin
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additional information
DNase1/3-like nuclease is inhibited by proteolysis of DNA-bound structural proteins but not by thrombin. When serum frozen at -20°C to thawing to room temperature and subsequently stored at 4°C, it looses its DNase1/3-like activity within 2 weeks
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additional information
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DNase1/3-like nuclease is inhibited by proteolysis of DNA-bound structural proteins but not by thrombin. When serum frozen at -20°C to thawing to room temperature and subsequently stored at 4°C, it looses its DNase1/3-like activity within 2 weeks
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additional information
no inhibition by G-actin, due to exchange of Y65 to H65 and A114 to S114 compared to the other G-actin-sensitive mammalian enzymes
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additional information
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no inhibition by G-actin, due to exchange of Y65 to H65 and A114 to S114 compared to the other G-actin-sensitive mammalian enzymes
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