Information on EC 3.1.22.1 - deoxyribonuclease II

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.22.1
-
RECOMMENDED NAME
GeneOntology No.
deoxyribonuclease II
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-64-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
F09G8.2
SwissProt
Manually annotated by BRENDA team
K04H4.6
SwissProt
Manually annotated by BRENDA team
N2 Bristol strain
-
-
Manually annotated by BRENDA team
guinea pig
-
-
Manually annotated by BRENDA team
japanese quail
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SM-ZK
-
-
Manually annotated by BRENDA team
SM-ZK
-
-
Manually annotated by BRENDA team
snail
-
-
Manually annotated by BRENDA team
commercial enzyme
-
-
Manually annotated by BRENDA team
Ovis aries aries
sheep
-
-
Manually annotated by BRENDA team
Fischer
-
-
Manually annotated by BRENDA team
snail
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
bis(p-nitrophenyl) phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate:
show the reaction diagram
-
slow hydrolysis at optimal pH from 5.6 to 5.9
-
?
calf thymus DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
show the reaction diagram
-
-
-
-
?
chromatin + H2O
oligonucleotides + ?
show the reaction diagram
deoxyribonucleoside 5'-phosphates p-nitrophenyl esters + H2O
p-nitrophenol + deoxyribonucleoside 5'-phosphates
show the reaction diagram
-
-
-
?
DNA + H2O
3' phosphooligonucleotides
show the reaction diagram
-
-
-
?
DNA + H2O
3'-phosphooligonucleotide
show the reaction diagram
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
show the reaction diagram
DNA + H2O
?
show the reaction diagram
DNA + H2O
oligonucleotides + ?
show the reaction diagram
dsDNA + H2O
oligonucleotides + ?
show the reaction diagram
-
velocity of DNA degradtion is four times higher four dsDNA than for ssDNA
-
-
?
duplex-oligonucleotide + H2O
?
show the reaction diagram
-
20- and 16mers with specific sequences and structures like hairpin and duplex DNA, can cut bonds in a loop at nearly the same rate as in duplex DNA, doesn't require phosphate exposure or a double-stranded track
-
?
d[ApAp(S)ApA] + H2O
d[Ap(S)ApA] + 3'-dAMP
show the reaction diagram
-
digestion of Rp- and Sp-isomers
after 2 h incubation, prolonged incubation leads to d[Ap(S)Ap]-Rp-isomer, dA and d[Ap(S)Ap]-Sp-isomer. Does not hydrolyse phosphorothioate internucleotidic linkage of either configuration
?
d[ApApApA] + H2O
d[ApApA] + 3'-dAMP
show the reaction diagram
-
-
after 60 min of incubation, prolonged incubation leads to 3'-dAMP and dA end products in a 3 : 1 ratio
?
linearized plasmid DNA + H2O
oligonucleotides + ?
show the reaction diagram
-
-
-
?
nuclei + H2O
oligonucleotides + ?
show the reaction diagram
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
plasmid DNA + H2O
?
show the reaction diagram
salmon testicular DNA + H2O
?
show the reaction diagram
-
-
-
-
?
ssDNA + H2O
oligonucleotides + ?
show the reaction diagram
-
velocity of DNA degradtion is four times higher four dsDNA than for ssDNA
-
-
?
supercoiled plasmid DNA + H2O
linearized plasmid DNA + ?
show the reaction diagram
-
-
-
?
supercoiled plasmid DNA + H2O
relaxed plasmid DNA + ?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
DNA + H2O
3'-phosphooligonucleotide
show the reaction diagram
-
using TdT-mediated dUTP-nicked-end labelling, TUNEL, is followed DNA fragmentation that occurs in vivo during programmed cell death, Nuc-1 functions in the elimination of TUNEL-reactive DNA ends to a TUNEL nonreactive state
-
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
show the reaction diagram
DNA + H2O
?
show the reaction diagram
-
the enzyme could be one of the factors in the late block to polyspermy in the cytoplasm of avian eggs, the enzyme activity might also be responsible for poor efficiency in obtaining transgenic birds by microinjection of exogenous DNA into the fertilised chick ovum
-
?
DNA + H2O
oligonucleotides + ?
show the reaction diagram
nuclei + H2O
oligonucleotides + ?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
more than 50% activation at 10 mM
Co2+
-
slight activation at 10 mM, inhibition at higher concentrations
CuCl2
-
high concentrations cause cyclic changes in the enzyme activity, the changes of enzyme activity are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants in vivo
CuSO4
-
high concentrations cause cyclic changes in the enzyme activity, the changes of enzyme activity are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants in vivo
Mn2+
-
slight activation at 10 mM, inhibition at higher concentrations
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
little effect on activity at 10 mM
actinomycin D
-
strong inhibition, coupling to the substrate not to the enzyme
Alkylating agents
-
-
-
aurintricarboxylic acid
-
-
bovine serum albumin
-
Ca2+
-
strong inhibition
CaCl2
-
above 200 mM
copper sulphate
-
suppresses enzyme activity in hemocytes
Cu2+
-
complete inhibition
DNA
-
inhibitory above 0.4 mg/ml
EDTA
-
dialysis of IgGs from rabbits immunized with DNase II against a buffer containing EDTA or addition of EDTA to the reaction mixture leads to a complete disappearance of DNase activity
Fe3+
-
complete inhibition at 0.1 mM
growth hormone
-
in mice fed a 20% protein diet, growth hormone treatment decreases elevated activites of DNase II and RNase
-
HPO42-
-
slightly inhibitory above pH 5.0
human growth hormone
-
treatment of post-weaning mice results in 63% inhibition in gastrocnemius muscle
-
iodoacetamide
-
slight inhibitory
iodoacetate
KCl
-
above 300 mM
MgCl2
-
above 150 mM
Mn(CH3COO)2
-
32% inhibition at 20 mM
MnCl2
-
above 200 mM
N-bromosuccinimide
-
strong inhibitory
N-ethylmaleimide
-
little effect on activity at 10 mM
Na2SO4
Protein inhibitor
-
inhibition below pH 5.6, forming a DNase-inhibitor complex
-
RNAi
-
expression of a DNase II–RNAi construct in flies results in a significant decrease in total hemocyte numbers
-
rRNA
-
specific competitive inhibition
SO42-
succinate buffer
-
activity less than 3% of that in acetate buffer at pH 5.0
-
tunicamycin
Zn(CH3COO)2
-
67% inbhibition at 20 mM
Zn2+
-
strong inhibition
ZnCl2
-
above 150 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AM-2282
-
-
AP-24
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apoptotic protease of 24 kDa, is activated during apoptosis and is able to activate L-DNase II
-
bromobenzene
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the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
cathepsin D
-
an acid protease, can transform LEI into L-DNase II
-
chlorobenzene
-
the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
copper sulphate
-
increases enzyme activity in the digestive gland
cysteine
-
protects the enzyme against traces of heavy metals
gasoline
-
increases enzyme activity in the digestive gland and in hemocytes
-
intracellular elastase
-
a neutral protease, can transform LEI into L-DNase II
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iodobenzene
-
the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
phenol
-
the changes of enzyme activity in vivo are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000005 - 0.0000608
supercoiled plasmid DNA
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000000183 - 0.00000167
supercoiled plasmid DNA
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
-
-
0.42 - 0.51
-
-
4.4
-
1fold purified
138
-
mutant H207L, pH 4.7
172
-
mutant H274L, pH 4.7
219
-
mutant H206L, pH 4.7
220
-
mutant H41L, pH 4.7
287
-
mutant H109L, pH 4.7
321
-
wild-type, pH 4.7
327.1
-
74.3fold purified
331
-
mutant H322L, pH 4.7
302000
-
pH 5.0
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.1
-
-
4.2 - 4.7
-
-
4.2 - 4.9
-
-
4.5 - 5
-
-
5.1 - 5.3
-
in acetate buffer
5.6
-
substrate ssDNA
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 6.5
-
-
4 - 7.5
-
pH 4.0: about 30% of maximal activity, pH 7.5: about 45% of maximal activity
4.7
-
hydrolyzes DNA under acidic conditions
5 - 6.8
-
pH 5.0: about 40% of maximal activity, pH 6.8: about 15% of maximal activity
7 - 8
pH 7.0: about 65% of maximal activity, pH 8.0: about 40% of maximnal activity
7.2
-
no activity above
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 55
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 70
-
40°C: about 70% of maximal activity, 70°C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
specific activity of acid DNase of unexposed, control mussels is higher in the hemocytes than in the digestive gland
Manually annotated by BRENDA team
-
embryo
Manually annotated by BRENDA team
-
multiple isoforms
Manually annotated by BRENDA team
-
isoform DNase II and acid RNase directly participate in muscle DNA and RNA degradation. Treatment with recombinant human growth hormone leads to 63% inhibition of DNase and 48% inhibition of RNase activity
Manually annotated by BRENDA team
-
somato-lactotrope cell
Manually annotated by BRENDA team
-
specific activity of acid DNase of unexposed, control mussels is higher in the hemocytes than in the digestive gland
Manually annotated by BRENDA team
-
low levels
Manually annotated by BRENDA team
-
low levels
Manually annotated by BRENDA team
-
low levels
Manually annotated by BRENDA team
-
low levels
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
during early differentiation, localization to lysosome. Later, an increasing portion of enzyme is found in cytosol
Manually annotated by BRENDA team
-
45-kDa form of recombinant DNase II
-
Manually annotated by BRENDA team
-
fraction of procaspase-8 and LEI colocalise in the mitochondria. After etoposide treatment, cathepsin D is released from lysosomes and part of it colocalises with caspase-8 and LEI
Manually annotated by BRENDA team
-
mitochondrial-lysosomal fraction
-
Manually annotated by BRENDA team
additional information
-
putative leucine-rich nuclear export signal on LEI/L-DNase II sequence, a mandatory condition for binding exportin molecules. The exportin Crm1 interacts with LEI/L-DNase II
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
gel filtration, SDS-PAGE
31000
-
gel filtration
32000
-
1 * 8000-10000 + 1 * 32000 + 1 * ?, cDNA and protein sequence analysis
34000
-
x * 34000, SDS-PAGE
37000
-
unglycosylated form of wild-type enzyme and N69Q mutant upon tunicamycin treatment
38030
-
calculation from cDNA sequence
38210
-
sequence analysis
40000
-
-
41000
-
gel filtration
42000 - 44000
-
SDS-PAGE, mature protein
43000
-
mutants N86Q, N212Q, N266Q, N290Q. It appears that the four sites each contribute to glycosylation and no additional glycosylation sites are responsible for the observed size
45000 - 46000
-
gel filtration, SDS-PAGE
46500
-
Western blot analysis or calculated (addition of the mass of sugar contents to the sequence-derived mass)
47000
-
D107N mutant, addition of glycosylation site
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 42000, SDS-PAGE
trimer
-
1 * 8000-10000 + 1 * 32000 + 1 * ?, cDNA and protein sequence analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structural model of protein. DNase IIalpha is a monomeric enzyme with pseudodimeric fold. It contains two requisite PLD-signature motifs in the N-terminal subdomains which together form a single active site
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
no inactivation during incubation at 0°C or 30°C
134306
8.5
-
inactivation at 30°C, not at 0°C
134306
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
the activity completely disappears after heating for 15 min
100
-
irreversible loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of bovine serum albumin stabilizes enzyme activity at 37°C
-
enzyme aggregates at low temperatures
-
resistant to heat and to incubation with proteinase K
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
polyethyleneglycol
-
activity remaines unchanged when stored at -40°C for 12 months
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the treatment with a reducing agent destroys the activity
-
650883
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl, pH 7.4, 5 mM 2-mercaptoethanol, 1 mM EDTA, 1 mM PMSF, 50% glycerol v/v, several months
-
8°C, 0.4 M NaCl, 0.05 M acetate, pH 5.5, one third of activity after 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by His-select cartridges
-
commercially available DNase II further purified by affinity chromatography
-
commercially available DNase II further purified by chromatography steps to homogeneity
-
near homogeneity by 3step chromatography techniques
-
near homogeneity by 5step chromatography techniques
-
near homogeneity by chromatography steps
near homogeneity by chromatography steps and isoelectric focusing
-
partial
partial purification using Con A Sepharose
-
to homogeneity by 4-6step chromatography techniques
-
to homogeneity by 4step chromatography techniques
-
to homogeneity by 6step chromatography techniques
to homogeneity by chromatography steps and isoelectric focusing
-
to homogeneity by chromatography techniques
-
to homogeneity by gel filtration, 74.3fold purified
-
to homogeneity by sucrose centrifugation steps and chromatography steps
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA of pDNase II cloned in the pcDNA3 vector and transfected into HEK 293T cells
-
DNA fragment containing the entire coding sequence of DNase II cDNA amplified and ligated into pcDNA3.1(+). Mutants corresponding to each single nucleotide polymorphism expressed in COS-7 cell
-
Escherichia coli BL21(DE3) pLysS strain transformed with a pET 23d(+) plasmid coding for LEI with a 6x His tag. PZeo-LEI wild-type transfected into HeLa cells, MEF cell lines or BHK-21 cells
-
expression in Chinese hamster ovary cells
-
expression in Chinese hamster ovary cells; expression in COS-7 cells
-
expression in COS-7 cells
-
expression in human embryonic kidney 293 cells
LEI cDNA subcloned into pZeoSV2+, into pET23d+ in frame with the His-tag, and into pDsRed2-C1 plasmid in frame with the red fluorescent protein fused to its N-term. Expression in Escherichia coli strain BL21(DE3) pLysS. BHK cells transfected with a pZeo vector containing the wild-type or a punctually mutated LEI cDNA
-
MEF-/- cells null for enzyme expression and activity are transiently transfected with plasmid-expression constructs encoding wild-type human DNase IIalpha, pD2, or mutant forms
-
nuc-1, crn-7 or crn-6 coding sequence without a stop codon amplified and inserted into the pPD95.79 vector. Transcriptional reporter constructs containing the promoter of the DNase II gene fused to GFP with four tandem copies of the nuclear localization signal (NLS) injected into wild-type animals (embryos, larvae and adults)
-
Sp1 and Sp3 play a pivotal role in the transcriptional activation of DNase II in HL-60 cells during phorbol 12-myristate-13-acetate induced differentiation
-
the C07B5.5 gene encodes the NUC-1 apoptotic nuclease
-
the gene encoding DNase IIbeta has identical splice sites to DNase IIalpha
-
the subsequent targeted disruption of the DNase II gene confirms the requirement of DNase II activity within phagocytic cells
-
the wild-type and mutant enzyme cDNA plasmid are transiently transfected in HCT116 cells
wild-type or mutant LEI expressed in BHK-21 cells. 6xHis tagged wild-type and mutant LEI expressed from pET 23d(+) plasmid in Escherichia coli BL21(DE3)pLysS strain. Wild-type LEI expressed in HeLa cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
during interdigital tissue regression process
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A335Term
-
does not eliminate DNase II activity
A58del
-
in Japanese, African, Korean and Caucasian subjects, homozygous for the G292 allele. Shows almost no DNase II activity
C11A
-
the mutation decreases the activity
C159A
-
complete loss of activity
C19A
-
complete loss of activity
C267A
-
complete loss of activity
C299A
-
the mutation increases the activity
C308A
-
complete loss of activity
C327A
-
complete loss of activity
C347A
-
complete loss of activity
D107N
-
although the mutant is capable of even greater glycosylation, this mutant results in some loss of activity
H188A
-
shows similar levels of activity to that of the wild-type
H188K
-
shows similar levels of activity to that of the wild-type
H188R
-
in Japanese, African, Korean and Caucasian subjects, homozygous for the A683 allele. DNase II activity is similar to that of the wild-type
N212Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N266Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N290Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N69Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
N86Q
-
mutation decreases activity, tunicamycin treatment results in complete loss of activity
Q322Term
-
eliminates DNase II activity; in Japanese, African, Korean and Caucasian subjects, homozygous for the C1084 allele. Shows almost no DNase II activity
Q329Term
-
eliminates DNase II activity
R23A
-
exerts no effect on the DNase II activity
R23H
-
exerts no effect on the DNase II activity
R23I
-
in Japanese, African, Korean and Caucasian subjects, homozygous for the G188 allele. DNase II activity is similar to that of the wild-type
R298A
-
drastically abrogates DNase II activity
R298H
-
drastically abrogates DNase II activity
R298K
-
drastically abrogates DNase II activity
R298L
-
in Japanese, African, Korean and Caucasian subjects, homozygous for the G1013 allele. Reduces the DNase II activity greatly to less than 10% of that of the wild-type
V190I
-
in Korean subjects,heterozygous for the G688 and A688 alleles. In Japanese, homozygous for the G688 allele. DNase II activity is similar to that of the wild-type
V284A
-
activity remains low
V284L
-
activity remains low
V284M
-
in Japanese, African, Korean and Caucasian subjects, homozygous for the G970 allele. Reduces the DNase II activity greatly to less than 10% of that of the wild-type
AP10T
-
point mutation in the hinge region of LEI, has decreased anti-protease activity. Cells overexpressing wild-type LEI or AP10T-LEI have the same survival rate under unstressed condition. Mutant retains its pro-apoptotic activity when transformed into L-DNase II by an apoptotic stimulus (e.g., hexa-methylene-amiloride treatment). When mutant cells are treated with etoposide they do not present the same survival rate than wild-type cells
H109L
-
extracellular, about 80% of wild-type activity
H115
-
extracellular, very little catalytic activity that may be rescued by imidazole, correct protein folding
H132L
-
soluble, very little catalytic activity. Protein is improperly folded and degraded via the proteosomal pathway within 24 h
H206L
-
extracellular, about 66% of wild-type activity
H207L
-
extracellular, about 40% of wild-type activity
H274L
-
extracellular, about 45% of wild-type activity
H297L
-
extracellular, very little catalytic activity that may be rescued by imidazole, correct protein folding
H322L
-
extracellular, activity similar to wild-type
H41L
-
extracellular, about 60% of wild-type activity
L286A
-
displays a decrease of survival compared to the wild-type
L290A
-
displays no decrease of survival compared to the wild-type
L293A
-
displays a decrease of survival compared to the wild-type
V295A
-
exhibits a significant cell death compared to the wild-type, highest rate of cells with nuclear retention of LEI
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
microtiter plate assay for quantification of enzyme activity in biological fluids. Assay is based on hydrolysis of 974 bp PCR product labeled with biotinylated forward and fluorescein-labeled reverse primers
medicine
additional information