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2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide + H2O
?
-
-
-
-
?
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide + H2O
?
-
-
-
-
?
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide + H2O
?
-
-
-
-
?
5-carboxyfluorescein-Lys-Lys-Ala-Ala-Glu-Ala-Ser-Lys-(QXL520)-OH + H2O
?
Abz-Glu-Ala-Leu-Gly-Thr-Ser-Pro-Arg-Lys(Dnp)-Asp + H2O
?
-
-
-
-
?
Abz-Glu-Gly-Ile-Gly-Thr-Ser-Arg-Pro-Lys(Dnp)-Asp + H2O
?
-
-
-
-
?
alcohol dehydrogenase + H2O
alcohol dehydrogenase proteolytically cleaved into peptide fragments
alpha-1-antitrypsin + H2O
alpha-1-antitrypsin proteolytically cleaved into peptide fragments
-
limited proteolysis
-
-
?
alpha1-proteinase inhibitor + H2O
?
-
human protein, inactivation by SspA
-
-
?
benzyl-Tyr-OEt + H2O
?
-
-
-
-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
Bz-Pro-Phe-Arg + 4-nitroaniline
casein + H2O
casein proteolytically cleaved into peptide fragments
elastin + H2O
elastin proteolytically cleaved into peptide fragments
-
insoluble substrate
-
-
?
fibrinogen A alpha chain + H2O
?
Gelatin + H2O
?
-
staphopain B
-
-
?
hemoglobin + H2O
hemoglobin proteolytically cleaved into peptide fragments
HMW-kininogen + H2O
HMW-kininogen proteolytically cleaved into peptide fragments
-
limited proteolysis
-
-
?
kininogen + H2O
kinin + ?
N-benzyloxycarbonyl-Phe-Leu-Glu-NH-p-nitroanilide + H2O
N-benzyloxycarbonyl-Phe-Leu-Glu + p-nitroaniline
-
-
-
-
?
N-Suc-Gly-Phe-Gly-p-nitroanilide + H2O
N-Suc-Gly-Phe-Gly + p-nitroaniline
peptide + H2O
amino acids
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
protein + H2O
peptide fragments
protein + H2O
protein proteolytically cleaved into peptide fragments
Z-Phe-Leu-Glu-p-nitroanilide + H2O
Z-Phe-Leu-Glu + p-nitroaniline
-
-
-
?
additional information
?
-
5-carboxyfluorescein-Lys-Lys-Ala-Ala-Glu-Ala-Ser-Lys-(QXL520)-OH + H2O
?
-
substrate for ScpA
-
-
?
5-carboxyfluorescein-Lys-Lys-Ala-Ala-Glu-Ala-Ser-Lys-(QXL520)-OH + H2O
?
-
substrate for ScpA
-
-
?
alcohol dehydrogenase + H2O
alcohol dehydrogenase proteolytically cleaved into peptide fragments
-
-
-
-
?
alcohol dehydrogenase + H2O
alcohol dehydrogenase proteolytically cleaved into peptide fragments
-
-
-
-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
?
-
substrate for SspB
-
-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
?
-
substrate for SspB
-
-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
Bz-Pro-Phe-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
Bz-Pro-Phe-Arg-4-nitroanilide + H2O
Bz-Pro-Phe-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
casein + H2O
casein proteolytically cleaved into peptide fragments
-
-
-
-
?
casein + H2O
casein proteolytically cleaved into peptide fragments
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
-
-
?
CXCR2 + H2O
?
-
the enzyme specifically cleaves the N-terminal domain of human CXCR2 between asparate-35 and alanine-36
-
-
?
CXCR2 + H2O
?
-
the enzyme specifically cleaves the N-terminal domain of human CXCR2 between asparate-35 and alanine-36
-
-
?
cystatin C + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin C + H2O
?
Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair function as protease inhibitor
-
-
?
cystatin C + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin C + H2O
?
Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair function as protease inhibitor
-
-
?
cystatin D + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
Ala10 bond hydrolyzed by staphopain A, truncation shown to impair inhibition of additional targets
-
-
?
cystatin D + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
Ala10 bond hydrolyzed by staphopain A, truncation shown to impair inhibition of additional targets
-
-
?
elastin agar + H2O
?
-
-
-
-
?
elastin agar + H2O
?
-
-
-
-
?
fibrinogen A alpha chain + H2O
?
-
rather slow degradation through Sscp A
-
-
?
fibrinogen A alpha chain + H2O
?
-
Sscp B cleaves the fibrinogen A alpha-chain at the C-terminal region very efficiently
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity
-
-
?
Galectin-3 + H2O
?
the enzyme inactivates galectin-3, abrogating its stimulation of oxygen radical production in human neutrophils and increasing tissue damage during skin infection
-
-
?
Galectin-3 + H2O
?
the enzyme inactivates galectin-3, abrogating its stimulation of oxygen radical production in human neutrophils and increasing tissue damage during skin infection
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity
-
-
?
hemoglobin + H2O
hemoglobin proteolytically cleaved into peptide fragments
-
-
-
-
?
hemoglobin + H2O
hemoglobin proteolytically cleaved into peptide fragments
-
-
-
-
?
integrin CD11b + H2O
?
-
on phagocytes
-
-
?
integrin CD11b + H2O
?
-
on phagocytes
-
-
?
kininogen + H2O
kinin + ?
-
activation of human protein by SspA, kinin generation is responsible for infection associated pain and endema
-
-
?
kininogen + H2O
kinin + ?
-
human protein, activation by SspA
-
-
?
milk agar + H2O
?
-
-
-
-
?
milk agar + H2O
?
-
-
-
-
?
N-Suc-Gly-Phe-Gly-p-nitroanilide + H2O
N-Suc-Gly-Phe-Gly + p-nitroaniline
-
characterization of a staphopain (StpA2aur CH-91) and its inhibitor (StpinA2aur CH-91) from a novel staphylococcal thiol protease operon (stpAB2CH-91), substrate used for inhibition studies
-
-
?
N-Suc-Gly-Phe-Gly-p-nitroanilide + H2O
N-Suc-Gly-Phe-Gly + p-nitroaniline
-
characterization of a staphopain (StpA2aur CH-91) and its inhibitor (StpinA2aur CH-91) from a novel staphylococcal thiol protease operon (stpAB2CH-91), substrate used for inhibition studies
-
-
?
peptide + H2O
amino acids
-
-
-
-
?
peptide + H2O
amino acids
-
broad specificity
-
-
?
peptide + H2O
amino acids
-
broad specificity
-
-
?
peptide + H2O
amino acids
-
-
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
-
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
broad specificity
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
-
-
-
?
protein + H2O
peptide fragments
-
-
-
-
?
protein + H2O
peptide fragments
-
broad specificity
-
-
?
protein + H2O
peptide fragments
-
broad specificity
-
-
?
protein + H2O
peptide fragments
-
-
-
-
?
protein + H2O
peptide fragments
-
-
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
-
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
broad specificity
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
enzyme may play a role in growth regulation
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
-
-
-
?
additional information
?
-
-
staphopains A and B are cysteine proteases, staphopain shows no activity with casein
-
-
?
additional information
?
-
staphopain B shown as a potent trigger of chemerin, the tazarotene-induced gene 2 protein TIG2, normally acting as a ligand for the G-protein coupled receptor CMKLR1, activation shown by proteolytic cleavage of the C-terminus
-
-
?
additional information
?
-
-
staphopain B shown as a potent trigger of chemerin, the tazarotene-induced gene 2 protein TIG2, normally acting as a ligand for the G-protein coupled receptor CMKLR1, activation shown by proteolytic cleavage of the C-terminus
-
-
?
additional information
?
-
-
staphopain A does not cleave human CXCR1
-
-
?
additional information
?
-
-
staphopain A does not cleave human CXCR1
-
-
?
additional information
?
-
staphopain B shown as a potent trigger of chemerin, the tazarotene-induced gene 2 protein TIG2, normally acting as a ligand for the G-protein coupled receptor CMKLR1, activation shown by proteolytic cleavage of the C-terminus
-
-
?
additional information
?
-
-
inhibitory interactions among staphopains and staphostatins determined, staphopain A of Staphylococcus epidermidis purified and used for interaction analysis
-
-
?
additional information
?
-
-
inhibitory interactions among staphopains and staphostatins determined and used for interaction analysis
-
-
?
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Collagen + H2O
?
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
-
-
?
kininogen + H2O
kinin + ?
-
activation of human protein by SspA, kinin generation is responsible for infection associated pain and endema
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
protein + H2O
protein proteolytically cleaved into peptide fragments
additional information
?
-
CXCR2 + H2O
?
-
the enzyme specifically cleaves the N-terminal domain of human CXCR2 between asparate-35 and alanine-36
-
-
?
CXCR2 + H2O
?
-
the enzyme specifically cleaves the N-terminal domain of human CXCR2 between asparate-35 and alanine-36
-
-
?
cystatin C + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin C + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
cystatin D + H2O
?
specificity of staphopains when interacting with cystatins as natural protein substrates presented
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity
-
-
?
Galectin-3 + H2O
?
the enzyme inactivates galectin-3, abrogating its stimulation of oxygen radical production in human neutrophils and increasing tissue damage during skin infection
-
-
?
Galectin-3 + H2O
?
the enzyme inactivates galectin-3, abrogating its stimulation of oxygen radical production in human neutrophils and increasing tissue damage during skin infection
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity
-
-
?
integrin CD11b + H2O
?
-
on phagocytes
-
-
?
integrin CD11b + H2O
?
-
on phagocytes
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
-
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
broad specificity
-
-
?
peptide + H2O
peptide proteolytically cleaved into fragments or single amino acids
-
-
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
-
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
broad specificity
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
enzyme may play a role in growth regulation
-
-
?
protein + H2O
protein proteolytically cleaved into peptide fragments
-
-
-
-
?
additional information
?
-
staphopain B shown as a potent trigger of chemerin, the tazarotene-induced gene 2 protein TIG2, normally acting as a ligand for the G-protein coupled receptor CMKLR1, activation shown by proteolytic cleavage of the C-terminus
-
-
?
additional information
?
-
-
staphopain B shown as a potent trigger of chemerin, the tazarotene-induced gene 2 protein TIG2, normally acting as a ligand for the G-protein coupled receptor CMKLR1, activation shown by proteolytic cleavage of the C-terminus
-
-
?
additional information
?
-
-
staphopain A does not cleave human CXCR1
-
-
?
additional information
?
-
-
staphopain A does not cleave human CXCR1
-
-
?
additional information
?
-
staphopain B shown as a potent trigger of chemerin, the tazarotene-induced gene 2 protein TIG2, normally acting as a ligand for the G-protein coupled receptor CMKLR1, activation shown by proteolytic cleavage of the C-terminus
-
-
?
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E64
-
ScpA-inhibitor binding structure
L-trans-epoxysuccinyl-leucylamide-(4-guanido)-butane
-
E-64, irreversible inhibitor
p-hydroxymercuribenzoate
-
-
phosphorylated cystatin alpha
-
from rat skin
-
squamous cell carcinoma antigen 1
-
the high association rate constant (kass) for inhibitory complex formation (19000 M/s for staphopain A interaction with SCCA1) suggests that squamous cell carcinoma antigen 1 (SCCA1) can regulate staphopain activity in vivo at epithelial surfaces infected/colonized by Staphylococcu aureus; the high association rate constant (kass) for inhibitory complex formation (58000 M/s for staphopain A interaction with SCCA1) suggests that squamous cell carcinoma antigen 1 (SCCA1) can regulate staphopain activity in vivo at epithelial surfaces infected/colonized by Staphylococcu aureus
-
staphostatins
-
co-expression of staphopain and inhibitor staphostatin from the same operon, regulatory effect; endogenous proteins that specifically inhibit staphopain; formation of tight and stable non-covalent complexes
-
alpha2-Macroglobulin
-
from human
-
alpha2-Macroglobulin
-
from human
-
E-64
-
stochiometrical and irreversible inhibition
Hg2+
-
-
staphostatin A
-
absolute specific for staphopain A; encoded by the gene scpB
-
staphostatin A
-
i.e. ScpB, intracellular, endogenous specific inhibitor of ScpA forming noncovalent complexes, structure determination, slight cleaving of the inhibitor by the enzyme
-
staphostatin B
-
endogenous inhibitor of cysteine proteases, recombinantly expressed in Escherichia coli as wild-type protein and mutant and purified; forms a mixed eight-stranded beta-barrel; structural interactions between inhibitor and enzyme are resolved from crystal structure of the enzyme-inhibitor complex
-
staphostatin B
-
absolute specific for staphopain B; encoded by the gene scpC
-
staphostatin B
-
i.e. SspC, intracellular, endogenous specific inhibitor of SspB forming noncovalent complexes, structure determination, slight cleaving of the inhibitor by the enzyme
-
staphostatin B
-
characterization of an endogenous staphostatin from Staphylococcus warneri and its target protease, in vivo assessment of inhibitory activities tested, inhibitor derived from one species of Staphylococcus can inhibit the staphopain from another species, inhibition only observed if both proteins belong to the same subgroup of either staphopain A/staphostatin A or staphopain B/staphostatin B orthologs
-
additional information
-
no inhibition by human kininogens and cystatin C
-
additional information
-
the proregion of the zymogen is inhibitory for the mature enzyme
-
additional information
-
inhibitory interactions among staphopains and staphostatins analyzed, inhibitor derived from one species of Staphylococcus can inhibit the staphopain from another species, in vivo assessment of inhibitory activities, inhibitory activities and stoichiometry presented
-
additional information
no inhibition of the cysteine proteases staphopain A by cystatin A, C, D and cystatin E/M, inhibitors shown to be hydrolyzed by staphopain A, inhibitory activity of native and staphopain-generated modified forms of cystatins presented; no inhibition of the cysteine proteases staphopain B by cystatin A, C, D and cystatin E/M, inhibitory activity of native and staphopain-generated modified forms of cystatins presented
-
additional information
no inhibition of the cysteine proteases staphopain A by cystatin A, C, D and cystatin E/M, inhibitors shown to be hydrolyzed by staphopain A, inhibitory activity of native and staphopain-generated modified forms of cystatins presented; no inhibition of the cysteine proteases staphopain B by cystatin A, C, D and cystatin E/M, inhibitory activity of native and staphopain-generated modified forms of cystatins presented
-
additional information
-
no inhibition of the cysteine proteases staphopain A by cystatin A, C, D and cystatin E/M, inhibitors shown to be hydrolyzed by staphopain A, inhibitory activity of native and staphopain-generated modified forms of cystatins presented; no inhibition of the cysteine proteases staphopain B by cystatin A, C, D and cystatin E/M, inhibitory activity of native and staphopain-generated modified forms of cystatins presented
-
additional information
-
immunglobulin G and immunglobulin G's Fc fragment reduce the effect of SspB
-
additional information
-
no inhibition by O-phenanthroline, diisofluorophosphate, phenylmethanesulfonyl fluoride, human kininogens and cystatins A,C, and D
-
additional information
-
staphostin homologue genes are probably encoding enzyme inhibitors
-
additional information
-
in vivo assessment of inhibitory activities determined, inhibitor derived from one species of Staphylococcus can inhibit the staphopain from another species, inhibition only observed if both proteins belong to the same subgroup of either staphopain A/staphostatin A or staphopain B/staphostatin B orthologs
-
additional information
-
staphostin homologue genes are probably encoding enzyme inhibitors
-
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0.0076 - 0.271
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
0.014 - 0.612
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
0.0056 - 0.385
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
0.033
cystatin C
Gly11 bond hydrolyzed by staphopain A, N-terminal truncation shown to impair inhibition of additional targets, disturbance of the host protease-inhibitor balance
-
0.032
cystatin D
Ala10 bond hydrolyzed by staphopain A, truncation of cystatin D shown to cause alleviated inhibition of endogenous target enzymes investigated, disturbance of the host protease-inhibitor balance
-
0.5
N-benzyloxycarbonyl-Phe-Leu-Glu-NH-p-nitroanilide
-
pH 8.0-8.8
3.3
N-Suc-Gly-Phe-Gly-p-nitroanilide
-
used as substrate for staphopain inhibition studies
0.0076
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.1639
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.271
2-aminobenzoyl-Ile-Ala-Ala-Gly-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain C
0.014
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain C
0.5871
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.612
2-aminobenzoyl-Ile-Ala-Lys-Asp-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.0056
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.154
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain A
0.385
2-aminobenzoyl-Phe-Gly-Ala-Lys-5-amino-2-nitrobenzoylamide
-
pH 7.6, 37°C, staphopain C
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additional information
-
cloning and characterization of staphopain A2 and its inhibitor from a novel staphylococcal thiol protease operon (stpAB2CH-91), staphopain/staphostatin interaction and evolution of encoding operons analyzed, evidence of ancestral allelic duplication and parallel evolution of the protease/inhibitor pairs suggested
additional information
cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by bacterial staphopains described, enzyme kinetic parameters shown
additional information
cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by bacterial staphopains described, enzyme kinetic parameters shown
additional information
-
cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by bacterial staphopains described, enzyme kinetic parameters shown
additional information
MALDI-TOF based time-course experiments of cleavage of cystatin C and D by staphopain A indicated, cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by staphopain A described, enzyme kinetic parameters shown
additional information
MALDI-TOF based time-course experiments of cleavage of cystatin C and D by staphopain A indicated, cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by staphopain A described, enzyme kinetic parameters shown
additional information
-
MALDI-TOF based time-course experiments of cleavage of cystatin C and D by staphopain A indicated, cystatin C assay to analyze the disturbance of the host protease-inhibitor balance by staphopain A described, enzyme kinetic parameters shown
additional information
proteolytic cleavage of the C-terminus of chemerin, the tazarotene-induced gene 2 protein TIG2, by staphopain B determined by SDS-PAGE, HPLC-analysis and MALDI-TOF, cell-activating potential of chemerin cleavage products determined, clinical isolates of Staphylococcus aureus shown to activate chemerin, activation determined in the presence of plasma inhibitors, no activation of chemerin by staphopain B mutants observed
additional information
-
proteolytic cleavage of the C-terminus of chemerin, the tazarotene-induced gene 2 protein TIG2, by staphopain B determined by SDS-PAGE, HPLC-analysis and MALDI-TOF, cell-activating potential of chemerin cleavage products determined, clinical isolates of Staphylococcus aureus shown to activate chemerin, activation determined in the presence of plasma inhibitors, no activation of chemerin by staphopain B mutants observed
additional information
-
peripheral blood neutrophils and monocytes exposed to SspB are extensively phagocytosed by resting human monocyte-derived macrophages in a time- and concentration-dependent manner. SspB-treated neutrophils engulfed in phagosomesstill preserve mitochondrial potential. SspB blocks phagocytosis of opsonised Staphylococcus aureus by neutrophils and monocytes. SspB blocks the chemotactic activity of neutrophils. SspB decreases surface expression of the major repulsion signal CD31 on neutrophils both in the absence and presence of human serum.
additional information
-
purified enzyme, spectrophotometrical assay
additional information
-
staphopain A of Staphylococcus epidermidis used for assessment of staphopain-staphostatin interactions, kinetics shown
additional information
-
ability of staphostatins to form a complex with the active site mutant C21A of Staphylococcus warneri staphopain determined by size exclusion chromatography
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