Information on EC 3.4.21.B7 - mannan-binding lectin-associated serine protease 1

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.B7
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
mannan-binding lectin-associated serine protease 1
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endopeptidase activity. It triggers the activation of complement cascade by activating the C4 and C2 components. It activates the C4 component by cleaving the alpha-chain of C4
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cleavage of C-N-linkage
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
214915-11-4
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-chain of complement C3 + H2O
?
show the reaction diagram
-
-
-
?
alpha-chain of complement C4 + H2O
?
show the reaction diagram
-
preferred substrate
-
?
antithrombin + H2O
?
show the reaction diagram
-
cleavage at R425-/-S425
-
-
?
benzoyl-L-arginine p-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
C1-inhibitor + H2O
?
show the reaction diagram
-
cleavage at R466-/-T467
-
-
?
complement component C2 + H2O
?
show the reaction diagram
complement component C2 + H2O
complement component C2b + ?
show the reaction diagram
-
-
-
-
?
complement component C3 + H2O
?
show the reaction diagram
complement component C3 + H2O
complement component C3a + complement component C3b
show the reaction diagram
-
activates complement C3
-
?
complement component C3 + H2O
complement component C3b + ?
show the reaction diagram
-
-
-
-
?
complement component C3i + H2O
?
show the reaction diagram
complement-activating component of Ra-reactive factor + H2O
?
show the reaction diagram
-
cleavage at Arg448-/-Ile449
-
-
?
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
show the reaction diagram
-
a chromogenic thrombin substrate, recombinant human mannose-binding lectin alone fails to cleave the substrate, but cleavage is restored when the recombinant enzyme MASP-1 is added to either MASP-1/-3 KO sera or rhMBL
-
-
?
factor D zymogen + H2O
mature factor D + ?
show the reaction diagram
-
-
-
-
?
factor XIII + H2O
?
show the reaction diagram
factor XIII + H2O
factor XIIIa + ?
show the reaction diagram
-
-
-
-
?
factor XIII A-chain + H2O
?
show the reaction diagram
-
catalytic activity for factor XIII and fibrinogen cleavage is much lower than that of thrombin
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
fibrinogen + H2O
fibrin + ?
show the reaction diagram
fibrinogen beta-chain + H2O
?
show the reaction diagram
-
cleavage at R44-/-G45 and other sites
-
-
?
high-molecular weight kininogen + H2O
bradykinin + ?
show the reaction diagram
-
a noncomplement substrate, activation
-
-
?
kininogen + H2O
bradykinin + ?
show the reaction diagram
-
-
-
-
?
kininogen + H2O
kinin + ?
show the reaction diagram
-
-
-
-
?
L-lysine thiobenzyl ester + H2O
?
show the reaction diagram
-
C3647
-
-
?
low-molecular-weight kininogen + H2O
?
show the reaction diagram
-
the cleavage rate of low-molecular-weight kininogen by MASP-1 is about 5times lower than that of kininogen
-
-
?
MASP-2 zymogen + H2O
mature MASP-2 + ?
show the reaction diagram
MASP-3 zymogen + H2O
mature MASP-3 + ?
show the reaction diagram
-
-
-
-
?
MASP1 mannan-binding lectin serine protease 1 isoform 1 precursor + H2O
?
show the reaction diagram
-
autodegradation pattern of the MASP-1 CCP1-CCP2-SP fragment. Cleavage occurs at the Arg504-Asp505 bond, which results in the removal of a 6000 Da fragment from the active enzyme. The autolysis of the MASP-1 CCP1-CCP2-SP fragment causes the loss of its enzymatic activity due to the removal of the histidine from the catalytic triad
-
-
?
N-carbobenzoxy-L-alanine-4-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
?
N-carbobenzoxy-L-lysine-4-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
?
N-carbobenzoxy-L-tyrosine-4-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
?
N-carboxybenzyloxyglycine-L-arginine thiobenzyl ester + H2O
?
show the reaction diagram
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
show the reaction diagram
-
-
-
?
PAR4 + H2O
?
show the reaction diagram
-
-
-
-
?
pro-factor D + H2O
factor D + ?
show the reaction diagram
proform coagulation factor XIII + H2O
mature coagulation factor XIII + ?
show the reaction diagram
proform factor XIII + H2O
mature factor XIII + ?
show the reaction diagram
proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
show the reaction diagram
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
show the reaction diagram
proform mannan-binding lectin-associated serine protease 3 + H2O
mature mannan-binding lectin-associated serine protease 3 + ?
show the reaction diagram
proform protease activated receptor 4 + H2O
mature protease activated receptor 4 + ?
show the reaction diagram
-
activation
-
-
?
proform thrombin-activatable fibrinolysis inhibitor + H2O
mature thrombin-activatable fibrinolysis inhibitor + ?
show the reaction diagram
protease activated receptor 4 + H2O
?
show the reaction diagram
protease-activated receptor 4 + H2O
?
show the reaction diagram
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
prothrombin + H2O
thrombin + ?
show the reaction diagram
prothrombin + H2O
thrombin a + ?
show the reaction diagram
Val-Pro-Arg-4-methylcoumarin-7-amide + H2O
?
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
complement component C2 + H2O
?
show the reaction diagram
complement component C3 + H2O
?
show the reaction diagram
-
-
-
-
?
factor D zymogen + H2O
mature factor D + ?
show the reaction diagram
-
-
-
-
?
factor XIII + H2O
?
show the reaction diagram
-
-
-
-
?
factor XIII + H2O
factor XIIIa + ?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
show the reaction diagram
high-molecular weight kininogen + H2O
bradykinin + ?
show the reaction diagram
-
a noncomplement substrate, activation
-
-
?
kininogen + H2O
bradykinin + ?
show the reaction diagram
-
-
-
-
?
low-molecular-weight kininogen + H2O
?
show the reaction diagram
-
the cleavage rate of low-molecular-weight kininogen by MASP-1 is about 5times lower than that of kininogen
-
-
?
MASP-2 zymogen + H2O
mature MASP-2 + ?
show the reaction diagram
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MASP-2 is a key enzyme that cleaves C4 and C2 to assemble a C3 convertase
-
-
?
MASP-3 zymogen + H2O
mature MASP-3 + ?
show the reaction diagram
-
-
-
-
?
pro-factor D + H2O
factor D + ?
show the reaction diagram
proform coagulation factor XIII + H2O
mature coagulation factor XIII + ?
show the reaction diagram
-
a noncomplement substrate, activation
-
-
?
proform factor XIII + H2O
mature factor XIII + ?
show the reaction diagram
-
activation
-
-
?
proform mannan-binding lectin-associated serine protease 1 + H2O
mature mannan-binding lectin-associated serine protease 1 + ?
show the reaction diagram
-
autocatalytic cleavage, a complement substrate, activation
-
-
?
proform mannan-binding lectin-associated serine protease 2 + H2O
mature mannan-binding lectin-associated serine protease 2 + ?
show the reaction diagram
proform mannan-binding lectin-associated serine protease 3 + H2O
mature mannan-binding lectin-associated serine protease 3 + ?
show the reaction diagram
-
a complement substrate, activation
-
-
?
proform protease activated receptor 4 + H2O
mature protease activated receptor 4 + ?
show the reaction diagram
-
activation
-
-
?
proform thrombin-activatable fibrinolysis inhibitor + H2O
mature thrombin-activatable fibrinolysis inhibitor + ?
show the reaction diagram
-
activation
-
-
?
protease activated receptor 4 + H2O
?
show the reaction diagram
-
PAR4, a noncomplement substrate, activation
-
-
?
protease-activated receptor 4 + H2O
?
show the reaction diagram
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
prothrombin + H2O
thrombin + ?
show the reaction diagram
prothrombin + H2O
thrombin a + ?
show the reaction diagram
-
enzyme MASP-1 cleaves prothrombinat three cleavage sites, MASP-1 gives rise to an alternative active form of thrombin by cleaving at the cleavage site R393
-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTRKLCW
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a Schistocerca gregaria protease inhibitor-1 P4-P4' sequence mutant
alpha-2-Macroglobulin
-
-
-
alpha2-Macroglobulin
-
may be a physiological inhibitor, 1-3fold molar excess, forms a stable complex with the enzyme
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antithrombin
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the inhibitior is not specific for MASP-1 versus MASP-2
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antithrombin III
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inhibitory in the presence of heparin on activity of MASP-1
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C1 inhibitor
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C1-inhibitor
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cyclic GICSRSLPPICIPD
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-
EDTA
-
inhibits binding of MASP-1 to immobilized mannan-binding lectin and L-ficolin/P35, when substituted for Ca2+
GICSRSLPPICIPD
-
-
lectin pathway C1-inhibitor
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the inhibitior is not specific for MASP-1 versus MASP-2
-
MCTRKLCW
-
a Schistocerca gregaria protease inhibitor-1 P4-P4' sequence mutant
MCTRKLCY
-
a Schistocerca gregaria protease inhibitor-1 P4-P4' sequence mutant
pefabloc
-
i.e. 4-(2-aminoethyl)-benzenesulphonyl fluoride
plasmaprotease C1-inhibitor
-
-
-
Schistocerca gregaria protease inhibitor-1
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Schistocerca gregaria protease inhibitor-2 variant FCTRKLCY
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randomization of positions P4, P2, P1, P1', P2', and P4' of the protease binding loop while keeping the structurally indispensable Cys at P3 and P3' leads to monospecific MASP inhibitors. Inhibitor variant FCTRKLCY is specific for isoform MASP-1, treatment completely blocks the lectin pathway activation, demonstrating that MASP-1 is not an auxiliary but an essential pathway component
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sunflower MASP inhibitor-1
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SFMI-1, sequence P4-P4' is ICSRSLPP
VCTRLWCE
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a sunflower MASP inhibitor-2 P4-P4' sequence mutant, only slight inhibition
VCTRLWCN
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a sunflower MASP inhibitor-2 P4-P4' sequence mutant, only slight inhibition
VCTRLYCN
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a sunflower MASP inhibitor-2 P4-P4' sequence mutant, only slight inhibition
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ficolin
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-
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mannan-binding lectin
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-
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mannose-binding lectin
-
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.9
benzoyl-L-arginine p-nitroanilide
-
cleavage by activated MASP-1 ent
13
complement C2
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cleavage by activated MASP-1 ent
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0.0048
Complement component C2
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37°C, cleavage by the MASP-1 CCP1-CCP2-SP fragment
-
1000
N-carbobenzoxy-L-alanine-4-nitrophenyl ester
-
pH 8, 25°C
20
N-carbobenzoxy-L-lysine-4-nitrophenyl ester
-
pH 6, 25°C
33
N-carbobenzoxy-L-tyrosine-4-nitrophenyl ester
-
pH 8, 25°C
0.31
N-carboxybenzyloxyglycine-L-arginine thiobenzyl ester
-
pH 7.4, 30°C
0.18
Nalpha-benzoyl-L-arginine ethyl ester
-
pH 7.4, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.3
benzoyl-L-arginine p-nitroanilide
Rattus norvegicus
-
cleavage by activated MASP-1 ent
3.9
complement C2
Rattus norvegicus
-
cleavage by activated MASP-1 ent
-
0.1
Complement component C2
Homo sapiens
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37°C, cleavage by the MASP-1 CCP1-CCP2-SP fragment
-
1.23 - 6.08
N-carboxybenzyloxyglycine-L-arginine thiobenzyl ester
0.35
Nalpha-benzoyl-L-arginine ethyl ester
Homo sapiens
-
pH 7.4, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30
Complement component C2
Homo sapiens
-
pH and temperature not specified in the publication
7369
6
complement component C3i
Homo sapiens
-
pH and temperature not specified in the publication
147868
0.4
high-molecular weight kininogen
Homo sapiens
-
pH and temperature not specified in the publication
99205
0.4
kininogen
Homo sapiens
-
recombinant MASP-1, at pH 7.8 and 37°C
4085
0.45
proform mannan-binding lectin-associated serine protease 1
Homo sapiens
-
pH and temperature not specified in the publication
202539
12
proform mannan-binding lectin-associated serine protease 2
Homo sapiens
-
pH and temperature not specified in the publication
202540
1.2
proform mannan-binding lectin-associated serine protease 3
Homo sapiens
-
pH and temperature not specified in the publication
202541
180
protease activated receptor 4
Homo sapiens
-
pH and temperature not specified in the publication
148565
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000027
ACTRKLCW
-
pH and temperature not specified in the publication, recombinant enzyme
0.000275
cyclic GICSRSLPPICIPD
-
in 20 mM HEPES, 145 mM NaCl, 5 mM CaCl2, and 0.05% (v/v) Triton X-100, at pH 7.6 and 22°C
0.000065
GICSRSLPPICIPD
-
in 20 mM HEPES, 145 mM NaCl, 5 mM CaCl2, and 0.05% (v/v) Triton X-100, at pH 7.6 and 22°C
0.00002
MCTRKLCW
-
pH and temperature not specified in the publication, recombinant enzyme
0.000014
MCTRKLCY
-
pH and temperature not specified in the publication, recombinant enzyme
0.000007
Schistocerca gregaria protease inhibitor-1
-
pH and temperature not specified in the publication, recombinant enzyme
-
0.000007
Schistocerca gregaria protease inhibitor-2 variant FCTRKLCY
-
pH not specified in the publication, temperature not specified in the publication
-
0.000065
sunflower MASP inhibitor-1
-
pH and temperature not specified in the publication, recombinant enzyme
0.153
VCTRLWCE
-
pH and temperature not specified in the publication, recombinant enzyme
0.087
VCTRLWCN
-
pH and temperature not specified in the publication, recombinant enzyme
0.176
VCTRLYCN
-
pH and temperature not specified in the publication, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
at physiological ionic strength, alternative pathway activity is observed, high ionic strength buffer suppresses the weaker alternative pathway activity of the Masp1 knockout mouse to background levels
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
SDS-PAGE and Western blot analysis, partially activated form
31000
-
1 * 66000 + 1 * 31000, activated form
32000
-
1 * 32000 + 1 * 34000, SDS-PAGE, reducing conditions
34000
-
1 * 32000 + 1 * 34000, SDS-PAGE, reducing conditions
38000
-
calculated molecular mass of the MASP-1 CUB-EGF fragment in the presence of Ca2+
50000
-
SDS-PAGE, non-reducing conditions
58000
-
1 * 58000 + 1 * 30000-32000, SDS-PAGE
65000
-
SDS-PAGE
66000
-
1 * 66000 + 1 * 31000, activated form
75000
-
x * 75000, SDS-PAGE
76980
-
calculated from sequence analysis
77040
-
calculated from nucleic acid sequence
81000
-
x * 81000, SDS-PAGE
87000
-
MASP-1, gel filtration
93000
-
unactivated proenzyme
100000
600000
-
large enzyme complexes in plasma, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
-
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic region of MASP-1, hanging-drop vapour-diffusion method, the best crystal diffract to 2.55 A resolution and belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.4, b = 70.4, c = 121.4 A
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hanging drop vapor diffusion method, X-ray structure of the CUB1-EGF-CUB2 domain of human MASP-1/3, responsible for interaction of MASP-1 and -3 with their partner proteins mannan-binding lectin and ficolins, is solved to a resolution of 2.3 A
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in complex with Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN, to 1.28 A resolution. Structure reveals significant plasticity of the protease; MASP-1 catalytic domain in complex with protease inhibitor SGPI-1, recombinant CCP1-CCP2-SP fragment of MASP-1 and SGMI-1 inhibitor are mixed in a 2:3 molar ratio and concentrated to 5 mg/ml, hanging drop vapor diffusion method, mixing of 0.001 ml of protein and 0.001 ml of reservoir solution comprising 0.1 M HEPES, pH 7.0, 25% PEG 1000, 0.3 M NaNO3, at 20°C, crystal structure determination and analysis at 3.2 A resolution, molecular replacement
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the collagen-like domain of mannan-binding lectin in complex with the binding domain of its associated protease MASP-1
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in diluted solutions
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography
mannan-agarose column chromatography
-
MBL-derivatized Sepharose column chromatography
-
partial
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recombinant wild-type and mutant MASP-1 catalytic fragments encoding the complement control protein domains 1 and 2, CCP1-CCP2-SP, region from Escherichia coli by repeated anion exchange chromatography and gel filtration
-
refolded recombinant chitin-binding domain-tagged MAPS-1 CUB1-EGF-CUB2 by anion echange chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic region of MASP-1 and MASP-2, consisting of the two CCP modules and the SP domain (CCP1-CCP2-SP) is expressed in Escherichia coli BL-21
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expressed in CHO cells
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expressed in HEK293 cells
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expressed in insect or human kidney cells
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expression in a baculovirus/insect cells system
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expression in Escherichia coli; expression of chitin-binding domain-tagged MAPS-1 CUB1-EGF-CUB2 construct in Escherichia coli strain BL21 (DE3) pLysS in inclusion bodies
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expression in HEK-293F FreeStyle cells
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expression of wild-type and catalytically inactive mutant full-length recombinant human MASP-1 entirely in the zymogen form in Hep-G2 and Chang liver cells or HEK-293F cells. The active protease is produced through co-expression with the serine protease inhibitor C1 inhibitor avoiding the self-suppression of enzyme expression by its autocatalytic activity, the expressed protease is capable of binding MBL and autoactivating, and is catalytically active
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expression oof MASP-1 catalytic fragments in Escherichia coli
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mature protein and truncated fragments
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recombinant expression of the CCP1-CCP2-SP fragment of enzyme MASP-1 in Escherichia coli
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recombinant expression of wild-type and mutant MASP-1 catalytic fragments encoding the complement control protein domains 1 and 2, CCP1-CCP2-SP, region (rMASPcf) in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the catalytic activity of MASP-1 suppresses its expression through rapid auto-activation and autodegradation intracellularly, not inhibited by addition of inhibitors to the culture medium
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R448Q
-
site-directed mutagenesis
R504Q
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site-directed mutagenesis, construction of a MASP-1 catalytic fragment, that has a molecular weight of 45.5 kDa and consists of the three C-terminal domains complement control protein 1 and 2 followed by the serine protease domain
S627A
-
kinetic parameters similiar to wild type, mutant is activated by its active counterpart
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
solubilization of recombinant chitin-binding domain-tagged MAPS-1 CUB1-EGF-CUB2 from Escherichia coli strain BL21 (DE3) pLysS inclusion bodies by 7 M guanidinium hydrochloride in 50 mM Tris, 50 mM DTT, pH 8.0, followed by dilution to 5.5 mg/ml protein, and refolding by diluting 20 ml of the 5 mg/mL solution into 1 l of 0.75 M Arg, 200 mM CaCl2, 3 mM glutathione, 2 mM oxidized glutathione, pH 8.0, refolding buffer, at least one week at 4°C, followed by dialysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
there is an association of higher MBL/MASP-1 complex activity with liver disease and an association with severity of fibrosis
additional information