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4-amino-benzene-His-Thr-Glu-Lys-leu-Val-Thr-Ser-dinitrophenol + H2O
?
-
-
-
-
?
Abz-His-Thr-Glu-Lys-Leu-Val-Thr-Ser-2,4-dinitrophenyl + H2O
Abz-His-Thr-Glu-Lys + Leu-Val-Thr-Ser-2,4-dinitrophenyl
-
-
-
-
?
albumin from chicken egg + H2O
?
lowest activity
-
-
?
alpha2-macroglobulin + H2O
fragments of alpha2-macroglobulin
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg
-
-
-
-
ir
bovine albumin + H2O
?
-
-
-
-
?
bovine fibrinogen + H2O
fibrin + ?
bovine gamma-globulin + H2O
?
-
-
-
-
?
bovine plasma fibrinogen + H2O
?
Bovine serum albumin + H2O
?
bovine serum gamma-globulin + H2O
?
-
marginal hydrolytic activity
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg
-
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
-
-
?
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
-
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
extracellular matrix component type VII collagen
?
-
-
-
-
?
factor Xa + H2O
?
-
-
-
-
?
Fibrin Aalpha-chain + H2O
?
-
human, cleavage at Lys413-Lys414, the Bbeta-chain is cleaved more slowly and the gamma-chain is minimally affected
-
-
?
fibrin clot + H2O
?
-
the enzyme induces inhibition of fibrin clot formation in a concentration-dependent manner
-
-
?
fibrinogen + H2O
fibrin + ?
fibrinogen + H2O
fibrin + propeptide
Fibrinogen Aalpha-chain + H2O
?
fibrinogen alpha chain + H2O
?
-
-
-
-
?
His-Thr-Glu-Ala-Leu-Val-Thr-Ser + H2O
?
His-Thr-Glu-Arg-Leu-Val-Thr-Ser + H2O
?
His-Thr-Glu-Asn-Leu-Val-Thr-Ser + H2O
?
His-Thr-Glu-Glu-Leu-Val-Thr-Ser + H2O
?
His-Thr-Glu-His-Leu-Val-Thr-Ser + H2O
?
His-Thr-Glu-Leu-Leu-Val-Thr-Ser + H2O
?
His-Thr-Glu-Lys-Ala-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Lys-Arg-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Lys-Asn-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Lys-Glu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Lys-His-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Lys-Leu-Val-Thr-Ser + H2O
?
His-Thr-Glu-Lys-Phe-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Lys-Pro-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Lys-Ser-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Phe-Leu-Val-Thr-Ser + H2O
?
His-Thr-Glu-Pro-Leu-Val-Thr-Ser + H2O
?
His-Thr-Glu-Ser-Leu-Val-Thr-Ser + H2O
?
Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val + H2O
?
low molecular weight kininogen + H2O
kallidin + ?
low-molecular weight kininogen + H2O
kallidin + ?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
second best substrate
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
plasminogen + H2O
plasmin + ?
pyroGlu-Gly-Arg-4-nitroanilide + H2O
pyroGlu-Gly-Arg + 4-nitroaniline
-
-
-
-
?
S-2444 + H2O
pyroGlu-Gly-Arg + 4-nitroaniline
-
i.e. pyroGlu-Gly-Arg-4-nitroanilide
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
thrombin + H2O
?
-
-
-
-
?
additional information
?
-
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
bovine fibrinogen + H2O
fibrin + ?
-
-
-
-
?
bovine fibrinogen + H2O
fibrin + ?
-
-
-
-
?
bovine fibrinogen + H2O
fibrin + ?
-
-
-
-
?
bovine plasma fibrinogen + H2O
?
-
marginal hydrolytic activity
-
-
?
bovine plasma fibrinogen + H2O
?
-
marginal hydrolytic activity
-
-
?
Bovine serum albumin + H2O
?
-
16.62% activity compared to human fibrin
-
-
?
Bovine serum albumin + H2O
?
-
16.62% activity compared to human fibrin
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
broad bean flour + H2O
?
-
-
-
-
?
broad bean flour + H2O
?
-
-
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
60.36% activity compared to human fibrin
-
-
?
casein + H2O
?
-
60.36% activity compared to human fibrin
-
-
?
casein + H2O
?
-
marginal hydrolytic activity
-
-
?
casein + H2O
?
-
marginal hydrolytic activity
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
highest activity
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
-
-
?
Fibrin + H2O
?
-
-
-
-
?
Fibrin + H2O
?
degradation of fibrin clots
-
-
?
Fibrin + H2O
?
-
fibrinolytic activity
-
-
?
Fibrin + H2O
?
fibrinolytic activity
-
-
?
Fibrin + H2O
?
-
fibrinolytic activity
-
-
?
Fibrin + H2O
?
-
fibrinolytic activity cleaving the Lys413-Leu414 bond
-
-
?
Fibrin + H2O
?
-
human substrate, fibrinolytic activity cleaving the Lys413-Leu414 bond
-
-
?
Fibrin + H2O
?
-
fibrinolase cleaves the alpha-chain more rapidly than the beta-chain of fibrin
-
-
?
Fibrin + H2O
?
-
the enzyme can catalyze fibrin clot lysis effectively
-
-
?
Fibrin + H2O
?
-
the enzyme can catalyze fibrin clot lysis effectively
-
-
?
Fibrin + H2O
?
-
the enzyme degrades all the four peptide chains of fibrin rapidly
-
-
?
Fibrin + H2O
?
-
the enzyme degrades all the four peptide chains of fibrin rapidly
-
-
?
Fibrin + H2O
?
-
the enzyme has the ability to directly degrade fibrin in vitro and effectively dissolve thrombi in vivo without activating plasminogen or influencing the activities of tissue plasminogen activator and plasminogen activator inhibitor-1
-
-
?
Fibrin + H2O
?
best substrate. The enzyme exhibits about 2fold higher activity for fibrin than fibrinogen. Fibrin can be hydrolyzed completely in about 30 min
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
fibrolase rapidly cleaves the A(alpha)-chain of fibrinogen and the B(beta)-chain at a slower rate, while it has no activity on the gamma-chain. The primary cleavage site at the alpha-chain ist he Lys-Leu bond at residues 413-414
-
-
?
Fibrinogen + H2O
?
the enzyme has a direct proteolytic activity against the A alpha-chain of fibrinogen at positions Lys413 and Leu414
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
55.21% activity compared to human fibrin. Among the three chains of fibrinogen, Aalpha and Bbeta chains are degraded rapidly, whereas gamma-chain of fibrinogen shows significant resistance to degradation by the enzyme
-
-
?
fibrinogen + H2O
fibrin + ?
-
the highest fibrinolytic activity and a degradation of blood clot in vitro of 62% are obtained in a medium with 2% (w/v) soybean flour and 1% (w/v) D-glucose at 200 rpm after 48 h of cultivation, at pH 7.2 and 37°C
-
-
?
fibrinogen + H2O
fibrin + ?
-
55.21% activity compared to human fibrin. Among the three chains of fibrinogen, Aalpha and Bbeta chains are degraded rapidly, whereas gamma-chain of fibrinogen shows significant resistance to degradation by the enzyme
-
-
?
fibrinogen + H2O
fibrin + ?
-
the highest fibrinolytic activity and a degradation of blood clot in vitro of 62% are obtained in a medium with 2% (w/v) soybean flour and 1% (w/v) D-glucose at 200 rpm after 48 h of cultivation, at pH 7.2 and 37°C
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
the enzyme degrades only Aalpha and Bbeta chains of fibrinogen
-
-
?
fibrinogen + H2O
fibrin + ?
-
the enzyme degrades only Aalpha and Bbeta chains of fibrinogen
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
the alpha-chain of fibrinogen is degraded very quickly within 5 min, followed by beta-chain in 1 h whereas the gamma-chain is degraded in 2 h
-
-
?
fibrinogen + H2O
fibrin + ?
-
the alpha-chain is rapidly hydrolyzed and the beta-chain is partially digested by 10 ng of starase. With an increase in starase concentration to 120 ng, the gamma-chain is partially degraded, but all the alpha-, beta- and gamma-chains of fibrinogen are completely cleaved by 250 ng and higher concentration of starase
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
fibrinogen can be hydrolyzed completely in 4-6 h
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
the enzyme exhibits cleavage of Aalphaand Bbeta chains of fibrin(ogen) and has no effect on gamma chain
-
-
?
fibrinogen + H2O
fibrin + propeptide
bovine substrate
-
-
?
fibrinogen + H2O
fibrin + propeptide
-
fibrinogenolytic activity
-
-
?
fibrinogen + H2O
fibrin + propeptide
bovine substrate, fibrinogenolytic activity
-
-
?
fibrinogen + H2O
fibrin + propeptide
-
human substrate, fibrinogenolytic activity
-
-
?
Fibrinogen Aalpha-chain + H2O
?
-
human
-
-
?
Fibrinogen Aalpha-chain + H2O
?
-
cleavage at Lys413-Leu414 (initial cleavage)
-
-
?
Fibrinogen Aalpha-chain + H2O
?
-
cleavage specificity is not dictated by the Lys-Leu bond per se, but by the surrounding sequence
-
-
?
Fibrinogen Aalpha-chain + H2O
?
-
the Bbeta-chain is cleaved more slowly and the gamma-chain is minimally affected
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
25.09% activity compared to human fibrin
-
-
?
Hemoglobin + H2O
?
-
25.09% activity compared to human fibrin
-
-
?
Hemoglobin + H2O
?
-
-
-
?
His-Thr-Glu-Ala-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Ala-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Arg-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Arg-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Asn-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Asn-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Glu-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Glu-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-His-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-His-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Leu-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Leu-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Lys-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Lys-Leu-Val-Thr-Ser + H2O
?
-
cleaving sequence residues 410-417 from fibrinogen Aalpha-chain
-
-
?
His-Thr-Glu-Phe-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Phe-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Pro-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Pro-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Ser-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
His-Thr-Glu-Ser-Leu-Val-Thr-Ser + H2O
?
-
-
-
-
?
human fibrin + H2O
?
-
fibrin is the most preferred substrate (100% activity). The beta-chain of fibrin is the primary component and site susceptible for the enzyme in early action. The enzyme can completely degrade all the four chains of fibrin
-
-
?
human fibrin + H2O
?
-
fibrin is the most preferred substrate (100% activity). The beta-chain of fibrin is the primary component and site susceptible for the enzyme in early action. The enzyme can completely degrade all the four chains of fibrin
-
-
?
Insulin B-chain + H2O
?
-
cleavage between Ala14 and Leu15
-
-
?
Insulin B-chain + H2O
?
-
oxidized
-
-
?
Insulin B-chain + H2O
?
-
fibrinogenolytic activity cleaving the Leu11-Val-Glu-Ala-Leu-Tyr-Leu-Val18 peptide
-
-
?
Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val + H2O
?
-
-
-
-
?
Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val + H2O
?
-
cleaving sequence residues 11-18 from insulin B-chain
-
-
?
low molecular weight kininogen + H2O
kallidin + ?
-
-
-
-
?
low molecular weight kininogen + H2O
kallidin + ?
-
-
i.e. Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
low molecular weight kininogen + H2O
kallidin + ?
-
-
-
-
?
low-molecular weight kininogen + H2O
kallidin + ?
-
-
-
-
?
low-molecular weight kininogen + H2O
kallidin + ?
-
initiates generation of bradykinin
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
marginal hydrolytic activity
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
marginal hydrolytic activity
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
additional information
?
-
-
no activity against a series of chromogenic 4-nitroanilide substrates
-
-
?
additional information
?
-
-
exhibits little if any hemorrhagic activity
-
-
?
additional information
?
-
-
does not activate protein C
-
-
?
additional information
?
-
-
does not activate plasminogen
-
-
?
additional information
?
-
-
does not activate plasminogen
-
-
?
additional information
?
-
-
direct fibrinolytic activity
-
-
?
additional information
?
-
fibrolase identified in multiple isoforms
-
?
additional information
?
-
-
fibrolase identified in multiple isoforms
-
?
additional information
?
-
-
thrombolysis in animals by snake venom alfimeprase, overview
-
-
?
additional information
?
-
-
alfimeprase is the recombinant truncated form of fibrolase from snake venom lacking the two N-terminal amino acids Glu and Gln
-
-
?
additional information
?
-
the enzyme is a nonhemorrhagic zinc metalloprotease
-
-
?
additional information
?
-
the enzyme is a nonhemorrhagic zinc metalloprotease
-
-
?
additional information
?
-
-
the enzyme is a nonhemorrhagic zinc metalloprotease
-
-
?
additional information
?
-
-
the enzyme is a nonhemorrhagic zinc metalloprotease, peptide substrate specificity, preference for Xaa-Leu and Xaa-Phe overview
-
-
?
additional information
?
-
chimeric Arg-Gly-Asp-fibrolase efficiently inhibits platelet aggregation in a dose-dependent manner and a prolonged incubation time obviously increased the inhibitory effect, in contrast to fibrolase
-
-
?
additional information
?
-
-
chimeric Arg-Gly-Asp-fibrolase efficiently inhibits platelet aggregation in a dose-dependent manner and a prolonged incubation time obviously increased the inhibitory effect, in contrast to fibrolase
-
-
?
additional information
?
-
-
fibrolase neither activates nor degrades plasminogen
-
-
?
additional information
?
-
-
no activity with plasminogen, N-benzoyl-Pro-Phe-Arg-4-nitroanilide, N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide, N-(4-tosyl)-Gly-Pro-Arg-4-nitroanilide, and bovine serum albumin
-
-
?
additional information
?
-
-
no activity with plasminogen, N-benzoyl-Pro-Phe-Arg-4-nitroanilide, N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide, N-(4-tosyl)-Gly-Pro-Arg-4-nitroanilide, and bovine serum albumin
-
-
?
additional information
?
-
-
no activity with Gly-Arg-4-nitroanilide and Nalpha-benzoyl-DL-Arg-4-nitroanilide
-
-
?
additional information
?
-
-
no activity with Gly-Arg-4-nitroanilide and Nalpha-benzoyl-DL-Arg-4-nitroanilide
-
-
?
additional information
?
-
-
the enzyme shows weak amidolytic activity for the substrates Z-D-Arg-Gly-Arg-4-nitroanilide and D-Phe-Pip-Arg-4-nitroanilide
-
-
?
additional information
?
-
-
the enzyme was devoid of hemorrhagic effect
-
-
?
additional information
?
-
-
the enzyme does not display any detectable hydrolysis of gamma chain of fibrin over a period of 180 min
-
-
?
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4-amidinophenylmethylsulfonyl fluoride
-
5% residual activity at 2 mM
4-bromophenacyl bromide
-
78.5% residual activity at 2 mM
acetaldehyde
-
about 3% activity at 2 mM
acetone
-
complete inhibition at 10% (v/v)
aprotin
84.1% residual activity at 1 mM
-
Ba2+
-
79.86% residual activity at 10 mM
bovine serum albumin
-
complete inhibition at 1% (w/v)
-
Cs2+
-
89.14% residual activity at 10 mM
CTAB
-
about 75% residual activity at 2 mM
cysteine
-
47.4% residual activity at 20 mM
disodium-EDTA
-
21.1% residual activity at 4 mM
DMSO
-
98.14% residual activity at 10 mM
ethanol
-
about 90% residual activity at 2 mM
Glutaraldehyde
-
about 5% residual activity at 2 mM
iodoacetamide
-
49.9% residual activity at 4 mM
iodoacetate
-
17.08% residual activity at 2 mM
L-lysine
-
38.5% residual activity at 5 mM
methanol
-
about 95% residual activity at 2 mM
N-4-tosyl-phenylalanyl chloromethyl ketone
-
16.5% residual activity at 0.1 mM
n-butanol
-
about 75% residual activity at 2 mM
Nalpha-tosyl-L-lysine chloromethylketone
-
51.5% residual activity at 0.1 mM
oxidized glutathione
-
complete inhibition at 5 mM
Pb2+
-
85.5% inhibition at 10 mM
pepstatin
-
71.5% residual activity at 2.5 mM
peptone
-
61.5% residual activity at 1% (w/v)
-
phenylmethane sulfonyl fluoride
-
-
phenylmethyl sulfonyl fluoride
-
about 90% residual activity at 2 mM
phenylmethylsulfonyl fluoride
protein SBTI
-
26% residual activity at 4 mM
-
reduced glutathione
-
complete inhibition at 5 mM
Soybean trypsin inhibitor
-
tetraethylene pentamine
-
rapid and complete inhibition
tosyl-L-lysine chloromethyl ketone
21.3% residual activity at 0.1 mM
tosyl-L-phenylalanine chloromethyl ketone
37.2% residual activity at 0.1 mM
tosyl-phenylalanine chloromethyl ketone
Triton X-100
-
87% residual activity at 0.01% (v/v)
Tween 20
-
80% residual activity at 0.01% (v/v)
Urea
-
complete inhibition at 8 M
1,10-phenanthroline
-
complete and rapid inhibition
1,10-phenanthroline
-
rapid and complete inhibition
1,10-phenanthroline
-
17.48% residual activity at 2 mM
2-mercaptoethanol
-
36.2% residual activity at 5 mM
2-mercaptoethanol
-
95.08% residual activity at 10 mM
2-mercaptoethanol
-
about 10% residual activity at 2 mM
2-mercaptoethanol
-
about 65% residual activity at 2 mM
Al3+
-
3.5% residual activity at 10 mM
Al3+
-
about 65% residual activity at 2 mM
Al3+
-
29% residual activity at 5 mM
Al3+
-
about 80% residual activity at 2 mM
alpha2-Macroglobulin
-
-
-
alpha2-Macroglobulin
-
the 720 kDa tetrameric inhibitor causes rapid and irreversible inhibition by sterical hindrance, the PEG-bound enzyme is less sensitive
-
alpha2-Macroglobulin
-
rapid, irreversible inhibition by physical entrapment
-
alpha2-Macroglobulin
-
-
-
Aprotinin
-
strong inhibition
Aprotinin
-
82.3% residual activity at 5 mM
Ca2+
-
87.04% residual activity at 10 mM
Ca2+
-
about 30% residual activity at 2 mM
Ca2+
-
88.8% residual activity at 1 mM
Co2+
-
48.3% residual activity at 5 mM
Co2+
-
21.6% inhibition at 10 mM
Co2+
-
61.59% residual activity at 10 mM
Co2+
60.4% residual activity at 1 mM
Co2+
-
60.8% residual activity at 1 mM
Co2+
-
about 80% residual activity at 2 mM
Cu2+
-
50% residual activity at 5 mM
Cu2+
-
4.55% residual activity at 10 mM
Cu2+
-
54.09% residual activity at 10 mM
Cu2+
-
61.2% residual activity at 5 mM
Cu2+
-
5.0% residual activity at 5 mM
Cu2+
50.1% residual activity at 1 mM
Cu2+
-
34.2% residual activity at 1 mM
Cu2+
-
32% residual activity at 5 mM
Cu2+
-
about 55% residual activity at 2 mM
dithiothreitol
-
84.92% residual activity at 10 mM
dithiothreitol
-
75% residual activity at 10 mM
dithiothreitol
-
92.8% residual activity at 4 mM
EDTA
-
complete and rapid inhibition
EDTA
-
EDTA sensitivity of the isoforms of the natural and of the recombinant enzyme
EDTA
-
rapid and complete inhibition
EDTA
-
10.4% residual activity at 5 mM
EDTA
-
2.15% residual activity at 10 mM
EDTA
-
67.85% residual activity at 5 mM
EDTA
-
13.5% residual activity at 5 mM
EDTA
-
16.51% residual activity at 2 mM
EDTA
-
6.25% residual activity at 5 mM
EDTA
77.5% residual activity at 5 mM
EDTA
-
39.9% residual activity at 10 mM
EDTA
-
45% residual activity at 1 mM
EDTA
-
complete inhibition at 2 mM
EGTA
-
strong inhibition
EGTA
74.7% residual activity at 5 mM
EGTA
-
36% residual activity at 1 mM
EGTA
-
complete inhibition at 2 mM
Fe2+
-
6.82% residual activity at 5 mM
Fe2+
-
52.95% residual activity at 10 mM
Fe2+
77.3% residual activity at 1 mM
Fe2+
-
95.3% residual activity at 1 mM
Fe2+
-
70% residual activity at 5 mM
Fe2+
-
complete inhibition at 2 mM
Fe3+
-
complete inhibition at 5 mM
Fe3+
-
about 40% residual activity at 2 mM
Fe3+
-
95.4% residual activity at 1 mM
Fe3+
-
36% residual activity at 5 mM
Hg2+
-
63% inhibition at 10 mM
Hg2+
-
17% residual activity at 5 mM
iodoacetic acid
-
80.54% residual activity at 10 mM
iodoacetic acid
-
96.42% residual activity at 10 mM
K+
-
98.6% residual activity at 5 mM
K+
-
86.69% residual activity at 10 mM
K+
-
30.9% inhibition at 10 mM
K+
-
93.86% residual activity at 2.5 mM
K+
-
about 80% residual activity at 2 mM
leupeptin
98.6% residual activity at 1 mM
leupeptin
-
about 75% residual activity at 2 mM
Mg2+
-
96.8% residual activity at 5 mM
Mg2+
-
92.64% residual activity at 10 mM
Mg2+
-
about 70% residual activity at 2 mM
Mg2+
-
94.4% residual activity at 1 mM
Mg2+
-
about 75% residual activity at 2 mM
Mn2+
-
strong inhibition
Mn2+
94.2% residual activity at 1 mM
Mn2+
-
about 70% residual activity at 2 mM
Na+
-
84.41% residual activity at 10 mM
Na+
-
91.59% residual activity at 2.5 mM
Na+
97.7% residual activity at 1 mM
Na+
-
about 85% residual activity at 2 mM
pepstatin A
-
48.2% residual activity at 5 mM
pepstatin A
-
84.31% residual activity at 10 mM
pepstatin A
-
91.3% residual activity at 5 mM
pepstatin A
95.2% residual activity at 1 mM
pepstatin A
-
14.6% residual activity at 1 mM
phenylmethylsulfonyl fluoride
-
8.48% residual activity at 5 mM
phenylmethylsulfonyl fluoride
-
8.62% residual activity at 10 mM
phenylmethylsulfonyl fluoride
-
42.85% residual activity at 5 mM
phenylmethylsulfonyl fluoride
-
52.9% residual activity at 2 mM
phenylmethylsulfonyl fluoride
-
complete inhibition at 5 mM
phenylmethylsulfonyl fluoride
-
4% residual activity at 2 mM
phenylmethylsulfonyl fluoride
18.5% residual activity at 1 mM
phenylmethylsulfonyl fluoride
-
25.4% residual activity at 50 mM
phenylmethylsulfonyl fluoride
-
28% residual activity at 4 mM
phenylmethylsulfonyl fluoride
-
about 70% residual activity at 2 mM
SDS
-
29% residual activity at 0.01% (w/v)
SDS
-
complete inhibition at 0.1% (w/v)
Soybean trypsin inhibitor
-
complete inhibition at 2 mM
-
Soybean trypsin inhibitor
28.2% residual activity at 1 mM
-
Tetraethylenepentamine
-
complete and rapid inhibition
Tetraethylenepentamine
-
-
tosyl-phenylalanine chloromethyl ketone
-
76.2% residual activity at 5 mM
tosyl-phenylalanine chloromethyl ketone
-
about 80% residual activity at 2 mM
Zn2+
-
52.6% residual activity at 5 mM
Zn2+
-
30% residual activity at 10 mM
Zn2+
-
about 80% residual activity at 2 mM
Zn2+
-
11% residual activity at 5 mM
Zn2+
67.6% residual activity at 1 mM
Zn2+
-
81.4% residual activity at 1 mM
Zn2+
-
42% residual activity at 5 mM
Zn2+
-
complete inhibition at 2 mM
additional information
-
not inhibited by any serine protease inhibitor
-
additional information
-
not: DFP, soybean trypsin inhibitor, trasylol, PCMB
-
additional information
-
polyethylene glycol addition to the enzyme modifies the enzyme size and reduces its activity
-
additional information
-
not inhibited by EDTA, iodoacetic acid, and 2-mercaptoethanol
-
additional information
-
not inhibited by EDTA and EGTA
-
additional information
-
not inhibited by iodoacetic acid
-
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Arthritis
Plasminogen is a joint-specific positive- or negative-determinant of arthritis pathogenesis.
Carotid Artery Thrombosis
Thrombolytic effects of recombinant fibrolase or APSAC in a canine model of carotid artery thrombosis.
Chickenpox
Gateways to clinical trials.
Cockayne Syndrome
Involvement of antipain-sensitive protease activity in the interferon-beta-induced UV-refractoriness of Cockayne syndrome fibroblasts.
Infections
Herpesviruses enhance fibrin clot lysis.
Infections
Toxoplasma gondii: effects of neuwiedase, a metalloproteinase from Bothrops neuwiedi snake venom, on the invasion and replication of human fibroblasts in vitro.
Influenza, Human
Gateways to clinical trials.
Ischemic Stroke
Alfimeprase.
Ischemic Stroke
Desmoteplase: discovery, insights and opportunities for ischaemic stroke.
Lung Injury
Adenovirally mediated gene transfer of functional human tissue-type plasminogen activator to murine lungs.
Myocardial Infarction
Defibrase, a purified fibrinolytic protease from snake venom in acute myocardial infarction.
Myocardial Infarction
Effect of thrombolysis on myocardial injury: recombinant tissue plasminogen activator vs. alfimeprase.
Myocardial Infarction
[Alterations of peripheral blood endothelial progenitor cells from patients with ST elevation myocardial infarction after snake venom fibrinolytic enzyme therapy.]
Myotoxicity
Pathological alterations induced by neuwiedase, a metalloproteinase isolated from Bothrops neuwiedi snake venom.
Neoplasms
The fibrinolysis inhibitor ?2-antiplasmin restricts lymphatic remodelling and metastasis in a mouse model of cancer.
Osteoporosis
Fibrin accumulation secondary to loss of plasmin-mediated fibrinolysis drives inflammatory osteoporosis.
Pulmonary Embolism
Starase: A bi-functional fibrinolytic protease from hepatic caeca of Asterina pectinifera displays antithrombotic potential.
Reperfusion Injury
Effect of thrombolysis on myocardial injury: recombinant tissue plasminogen activator vs. alfimeprase.
ST Elevation Myocardial Infarction
[Alterations of peripheral blood endothelial progenitor cells from patients with ST elevation myocardial infarction after snake venom fibrinolytic enzyme therapy.]
Stroke
Fibrolase: trials and tribulations.
Thromboembolism
Improved Reactive Oxygen Species Generation by Chiral Co3 O4 Supraparticles under Electromagnetic Fields.
Thrombosis
A phase I trial of alfimeprase for peripheral arterial thrombolysis.
Thrombosis
Alfimeprase: a novel recombinant direct-acting fibrinolytic.
Thrombosis
Alpha-fibrinogenases.
Thrombosis
Biological and thrombolytic properties of fibrolase--a new fibrinolytic protease from snake venom.
Thrombosis
Chimeric derivative of fibrolase, a fibrinolytic enzyme from southern copperhead venom, possesses inhibitory activity on platelet aggregation.
Thrombosis
Clinical utility of novel agents in the treatment of central venous catheter occlusion.
Thrombosis
Effect of thrombolysis on myocardial injury: recombinant tissue plasminogen activator vs. alfimeprase.
Thrombosis
Extracellular Production of a Potent and Chemically Resistant Nattokinase in Immobilized Escherichia coli Using Response Surface Methodology.
Thrombosis
Feedback regulation of endothelial cell surface plasmin generation by PKC dependent phosphorylation of annexin A2.
Thrombosis
Fibrolase: trials and tribulations.
Thrombosis
In Vivo Anticoagulant and Thrombolytic Activities of a Fibrinolytic Serine Protease (Brevithrombolase) With the k-Carrageenan-Induced Rat Tail Thrombosis Model.
Thrombosis
Preparation and toxicity evaluation of a novel nattokinase-tauroursodeoxycholate complex.
Thrombosis
Starase: A bi-functional fibrinolytic protease from hepatic caeca of Asterina pectinifera displays antithrombotic potential.
Thrombosis
The annexin A2/S100A10 system in health and disease: emerging paradigms.
Thrombosis
Thrombolytic effects of recombinant fibrolase or APSAC in a canine model of carotid artery thrombosis.
Thrombosis
Thrombolytic Potential of Novel Thiol-Dependent Fibrinolytic Protease from Bacillus cereus RSA1.
Venous Thrombosis
Alfimeprase.
Venous Thrombosis
Fibrolase, an active thrombolytic enzyme in arterial and venous thrombosis model systems.
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Guan, A.L.; Retzios, A.D.; Henderson, G.N.; Markland, F.S.
Purification and characterization of a fibrinolytic enzyme from venom of the southern copperhead snake (Agkistrodon contortrix contortrix)
Arch. Biochem. Biophys.
289
197-207
1991
Agkistrodon contortrix contortrix
brenda
Retzios, A.D.; Markland, F.S.
A direct-acting fibrinolytic enzyme from the venom of Agkistrodon contortrix contortrix: effects on various components of the human blood coagulation and fibrinolysis systems
Thromb. Res.
52
541-552
1988
Agkistrodon contortrix contortrix
brenda
Randolph, A.; Chamberlain, S.H.; Chu, H.L.C.; Retzios, A.D.; Markland, F.S.; Masiarz, F.R.
Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme from Agkistrodon contortrix contortrix venom
Protein Sci.
1
590-600
1992
Agkistrodon contortrix contortrix
brenda
Loayza, S.L.; Trikha, M.; Markland, F.S.; Riquelme, P.; Kuo, J.
Resolution of isoforms of natural and recombinant fibrolase, the fibrinolytic enzyme from Agkistrodon contortrix contortrix snake venom, and comparison of their EDTA sensitivities
J. Chromatogr.
662
227-243
1994
Agkistrodon contortrix contortrix
brenda
Retzios, A.D.; Markland, F.S.
Fibrinolytic enzymes from the venoms of Agkistrodon contortrix contortrix and Crotalus basiliscus basiliscus: cleavage site specificity towards the alpha-chain of fibrin
Thromb. Res.
74
355-367
1994
Agkistrodon contortrix contortrix
brenda
Manning, M.C.
Sequence analysis of fibrolase, a fibrinolytic metalloproteinase from Agkistrodon contortrix contortrix
Toxicon
33
1189-1200
1995
Agkistrodon contortrix contortrix
brenda
Trikha, M.; Schmitmeier, S.; Markland, F.S.
Purification and characterization of fibrolase isoforms from venom of individual southern copperhead (Agkistrodon contortrix Contortrix) snakes
Toxicon
32
1521-1531
1994
Agkistrodon contortrix contortrix
brenda
Patton, L.M.; Pretzer, D.; Schulteis, B.S.; Saggart, B.S.; Tennant, K.D.; Ahmed, N.K.
Activity assays for characterizing the thrombolytic protein fibrolase
J. Biochem. Biophys. Methods
27
11-23
1993
Agkistrodon contortrix contortrix
brenda
Markland, F.S.; Morris, S.; Deschamps, J.R.; Ward, K.B.
Resolution of isoforms of natural and recombinant fibrinolytic snake venom enzyme using high performance capillary electrophoresis
J. Liq. Chromatogr.
16
2189-2201
1993
Agkistrodon contortrix contortrix
-
brenda
Pretzer, D.; Schulteis, B.; Vander Velde, D.G.; Smith, C.D.; Mitchell, J.W.; Manning, M.C.
Effect of zinc binding on the structure and stability of fibrolase, a fibrinolytic protein from snake venom
Pharm. Res.
9
870-877
1992
Agkistrodon contortrix contortrix
brenda
Pretzer, D.; Schulteis, B.S.; Smith, C.D.; Vander Velde, D.G.; Mitchell, J.W.; Manning, M.C.
Stability of the thrombolytic protein fibrolase: effect of temperature and pH on activity and conformation
Pharm. Res.
8
1103-1112
1991
Agkistrodon contortrix contortrix
brenda
Chen, H.M.; Guan, A.L.; Markland, F.S.
Immunological properties of the fibrinolytic enzyme (fibrolase) from southern copperhead (Agkistrodon contortrix contortrix) venom and its purification by immunoaffinity chromatography
Toxicon
29
683-694
1991
Agkistrodon contortrix contortrix
brenda
Guan, A.L.; Markland, F.S.
Isoelectric focusing in immobilized pH gradients of a snake venom fibrinolytic enzyme
J. Biochem. Biophys. Methods
16
215-226
1988
Agkistrodon contortrix contortrix
brenda
Bolger, M.B.; Swenson, S.; Markland, F.S., Jr.
Three-dimensional structure of fibrolase, the fibrinolytic enzyme from southern copperhead venom, modeled from the X-ray structure of adamalysin II and atrolysin C
AAPS Pharmsci.
3
E16
2001
Agkistrodon contortrix contortrix (P28891), Agkistrodon contortrix contortrix
brenda
Swenson, S.; Toombs, C.F.; Pena, L.; Johansson, J.; Markland, F.S.
alpha-Fibrinogenases
Curr. Drug Targets Cardiovasc. Haematol. Disord.
4
417-435
2004
Agkistrodon contortrix
brenda
Swenson, S.; Markland, F.S.; Toombs, C.
Fibrolase
Handbook of Proteolytic Enzymes (Barrett,A. J. ;Rawlings,N. D. ,Woessner)
1
640-643
2004
Agkistrodon contortrix
-
brenda
Swenson, S.; Markland, F.S.
Snake venom fibrin(ogen)olytic enzymes
Toxicon
45
1021-1039
2005
Agkistrodon contortrix, Bothrops neuwiedi, Gloydius halys
brenda
Shi, J.; Zhang, S.T.; Zhang, X.J.; Xu, H.; Guo, A.G.
Expression, purification, and activity identification of alfimeprase in Pichia pastoris
Protein Expr. Purif.
54
240-246
2007
Agkistrodon contortrix contortrix (P28891)
brenda
Zhang, S.T.; Shi, J.; Zhao, J.; Qi, Y.F.; Guo, A.G.
Expression of soluble and functional snake venom fibrinolytic enzyme fibrolase via the co-expression of DsbC in Escherichia coli
Protein Pept. Lett.
13
559-563
2006
Agkistrodon contortrix contortrix (P28891), Agkistrodon contortrix contortrix
brenda
Swenson, S.; Markland, F.S.
Fibrolase
Toxin Rev.
25
351-378
2006
Agkistrodon contortrix contortrix
-
brenda
Toombs, C.F.; Deitcher, S.R.
Nonclinical and clinical characterization of a novel acting thrombolytic: alfimeprase
Toxin Rev.
25
379-392
2006
Agkistrodon contortrix contortrix
-
brenda
No authors listed
Alfimeprase
Drugs R. D.
9
185-190
2008
Agkistrodon contortrix contortrix
brenda
Verhamme, I.M.; Bock, P.E.
Rapid-reaction kinetic characterization of the pathway of streptokinase-plasmin catalytic complex formation
J. Biol. Chem.
283
26137-26147
2008
Homo sapiens
brenda
Lin, X.; Liang, X.; Tang, J.; Chen, J.; Qiu, P.; Yan, G.
The effect of the fibrinolytic enzyme FIIa from Agkistrodon acutus venom on acute pulmonary thromboembolism
Acta Pharmacol. Sin.
32
239-244
2011
Deinagkistrodon acutus
brenda
Fang, H.M.; Zhao, L.; Lu, P.; Chen, S.J.; Bao, Z.X.; Qin, Y.F.; Zhu, Z.Y.; Zhao, J.M.; Mai, J.; Zhang, S.T.
Modular design, expression and characterization of novel bifunctional mutants of fibrolase with combined platelet aggregation-inhibition and fibrinolytic activity
Protein J.
30
247-252
2011
Agkistrodon contortrix contortrix (P28891), Agkistrodon contortrix contortrix
brenda
Markland, F.S.; Swenson, S.
Fibrolase: trials and tribulations
Toxins
2
793-808
2010
Agkistrodon contortrix contortrix
brenda
Bajaj, B.; Sharma, N.; Singh, S.
Enhanced production of fibrinolytic protease from Bacillus cereus NS-2 using cotton seed cake as nitrogen source
Biocatal. Agricult. Biotechnol.
2
204-209
2013
Bacillus cereus, Bacillus cereus NS-2
-
brenda
Majumdar, S.; Sarmah, B.; Gogoi, D.; Banerjee, S.; Ghosh, S.; Banarjee, S.; Chattopadhyay, P.; Mukherjee, A.
Characterization, mechanism of anticoagulant action, and assessment of therapeutic potential of a fibrinolytic serine protease (Brevithrombolase) purified from Brevibacillus brevis strain FF02B
Biochimie
103
50-60
2014
Brevibacillus brevis, Brevibacillus brevis FF02B
brenda
Choi, J.; Sapkota, K.; Kim, S.; Kim, S.
Starase: A bi-functional fibrinolytic protease from hepatic caeca of Asterina pectinifera displays antithrombotic potential
Biochimie
105
45-57
2014
Patiria pectinifera
brenda
Bi, Q.; Han, B.; Liu, W.; Feng, Y.; Jiang, Z.
UFEIII, a fibrinolytic protease from the marine invertebrate, Urechis unicinctus
Biotechnol. Lett.
35
1115-1120
2013
Urechis unicinctus
brenda
Bajaj, B.; Singh, S.; Khullar, M.; Singh, K.; Bhardwaj, S.
Optimization of fibrinolytic protease production from Bacillus subtilis I-2 using agro-residues
Braz. Arch. Biol. Technol.
57
653-662
2014
Bacillus subtilis, Bacillus subtilis I-2
-
brenda
Silva, G.; Bezerra, R.; Teixeira, J.; Porto, T.; Lima-Filho, J.; Porto, A.
Fibrinolytic protease production by new Streptomyces sp. DPUA 1576 from Amazon lichens
Electron. J. Biotechnol.
18
16-19
2015
Streptomyces sp.
-
brenda
Bagchi, S.; Sondhia, S.; Agrawal, M.; Banerjee, S.
An angiotensin-converting enzyme-inhibitory metabolite with partial structure of microginin in a cyanobacterium Anabaena fertilissima CCC597, producing fibrinolytic protease
J. Appl. Phycol.
28
177-180
2016
Trichormus fertilissimus, Trichormus fertilissimus CCC597
-
brenda
Taneja, K.; Bajaj, B.; Kumar, S.; Dilbaghi, N.
Production, purification and characterization of fibrinolytic enzyme from Serratia sp. KG-2-1 using optimized media
3 Biotech
7
184
2017
Serratia sp. KG-2-1
brenda
Silva, G.; Bezerra, R.; Teixeira, J.; Silva, F.; Correia, J.; Porto, T.; Lima-Filho, J.; Porto, A.
Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens
Acta Amaz.
46
301-310
2016
Streptomyces sp. DPUA 1576
-
brenda
Xiao, P.; Yao, S.; Liu, J.; Miao, Y.; Wang, Y.
Enhanced production of fibrinolytic enzyme from Bacillus amyloliquefaciens CGMCC 7380 using broad bean (Vicia faba L.) as substrate
Adv. J. Food Sci. Technol.
9
832-839
2015
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens CGMCC 7380
-
brenda
Meshram, V.; Saxena, S.; Paul, K.; Gupta, M.; Kapoor, N.
Production, purification and characterisation of a potential fibrinolytic protease from endophytic Xylaria curta by solid substrate fermentation
Appl. Biochem. Biotechnol.
181
1496-1512
2017
Xylaria curta
brenda
Choi, J.; Lee, H.; Kim, S.
Purification and antithrombotic activity of wulfase, a fibrinolytic enzyme from the fruit bodies of the edible and medicinal mushroom Sparassis crispa Wulf. ex. Fr
Appl. Biochem. Microbiol.
52
608-614
2016
Sparassis crispa
-
brenda
Verma, P.; Chatterjee, S.; Keziah, M.S.; Devi, S.C.
Fibrinolytic protease from marine Streptomyces rubiginosus VITPSS1
Cardiovasc. Hematol. Agents Med. Chem.
16
44-55
2018
Streptomyces rubiginosus, Streptomyces rubiginosus VITPSS1
brenda
Yogesh, D.; Halami, P.
Evidence that multiple proteases of Bacillus subtilis can degrade fibrin and fibrinogen
Int. Food Res. J.
22
1662-1667
2015
Bacillus subtilis, Bacillus subtilis BR21
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brenda
Sun, Z.; Liu, P.; Cheng, G.; Zhang, B.; Dong, W.; Su, X.; Huang, Y.; Cui, Z.; Kong, Y.
A fibrinolytic protease AfeE from Streptomyces sp. CC5, with potent thrombolytic activity in a mouse model
Int. J. Biol. Macromol.
85
346-354
2016
Streptomyces sp. CC5 (A0A0A7W604)
brenda
Nascimento, T.; Sales, A.; Porto, C.; Brandao, R.; de Campos-Takaki, G.; Teixeira, J.; Porto, T.; Porto, A.; Converti, A.
Purification of a fibrinolytic protease from Mucor subtilissimus UCP 1262 by aqueous two-phase systems (PEG/sulfate)
J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.
1025
16-24
2016
Mucor subtilissimus, Mucor subtilissimus UCP 1262
brenda
Khobragade, C.; Gophane, S.; Motwani, R.
Purification and characterization of extracellular protease from soil isolate Stenotrophomonas maltophilia as novel target for fibrinolysis
J. Microbiol. Biotechnol. Food Sci.
7
496-502
2018
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia CNK-7R
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brenda
Liu, X.; Kopparapu, N.; Zheng, H.; Katrolia, P.; Deng, Y.; Zheng, X.
Purification and characterization of a fibrinolytic enzyme from the food-grade fungus, Neurospora sitophila
J. Mol. Catal. B
134
98-104
2016
Neurospora sitophila
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brenda
de Souza, F.; Sales, A.; Costa e Silva, P.; Bezerra, R.; de Medeiros e Silva, G.; de Arajo, J.; de Campos Takaki, G.; Porto, T.; Teixeira, J.; Porto, A.
Optimization of production, biochemical characterization and in vitro evaluation of the therapeutic potential of fibrinolytic enzymes from a new Bacillus amyloliquefaciens
Macromol. Res.
24
587-595
2016
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens UFPEDA 485
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brenda
D, D.; S, J.N.; S, M.K.; C, S.D.
Novel fibrinolytic protease producing Streptomyces radiopugnans VITSD8 from marine sponges
Mar. Drugs
17
164
2019
Streptomyces radiopugnans, Streptomyces radiopugnans VITSD8
brenda
Devaraj, Y.; Rajender, S.K.; Halami, P.M.
Purification and characterization of fibrinolytic protease from Bacillus amyloliquefaciens MCC2606 and analysis of fibrin degradation product by MS/MS
Prep. Biochem. Biotechnol.
48
172-180
2018
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens MCC2606
brenda