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53.8
-
Tbeta-kallikrein, pH 8.0, 25°C
62.5
-
alpha-kallikrein, pH 8.0, 25°C
81.6
-
Abeta-kallikrein, pH 8.0, 25°C
100
-
Cbeta-kallikrein, pH 8.0, 25°C
0.3
-
pH 8.0, 25°C, isoenzyme aT-II
10.5
-
enzyme with O-carboxymethyl-poly-beta-cyclodextrin attached to surface, pH 8.0, 25°C
12.3
-
wild-type, pH 8.0, 25°C
42.9
-
pH 8.0, 25°C, isoenzyme aT-I
2.6
-
pH 5.6, 25°C, in 0.3 M KCl
91
92
depending on assay method
0.03
-
mutant Q350A, pH 7.6, 37°C
0.03
-
pH 7.6, 37°C, mutant enzyme Q350A
0.04
-
mutant V469T, pH 7.5, 25°C
0.057
0.65
pH 7.6, 55°C, peptidylarginine deiminase 1
0.07
-
mutant R372A, pH 7.5, 25°C
0.1
-
mutant E412A, pH 7.6, 37°C
0.1
-
mutant V469L, pH 7.5, 25°C
0.1
-
pH 7.6, 37°C, mutant enzyme E412A
0.12
-
mutant R372Q, pH 7.5, 25°C
0.2
-
mutant R373A, pH 7.6, 37°C
0.2
-
pH 7.6, 37°C, mutant enzyme W373A
0.25
-
mutant E352A, pH 7.6, 37°C
0.25
-
pH 7.6, 37°C, mutant enzyme E352A
0.27
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.35
-
mutant D166A, pH 7.6, 37°C
0.35
-
pH 7.6, 37°C, mutant enzyme D166A
0.51
-
mutant D389A, pH 7.6, 37°C
0.51
-
pH 7.6, 37°C, mutant enzyme D389A
0.55
-
pH 7.6, 55°C, peptidylarginine deiminase 2
0.6
-
mutant D370A, pH 7.6, 37°C
0.6
-
mutant W548K, pH 7.5, 25°C
0.6
-
pH 7.6, 37°C, mutant enzyme D370A
0.8
-
mutant D123N, pH 7.6, 37°C
0.8
-
mutant D125A, pH 7.6, 37°C
0.8
-
mutant V469A, pH 7.5, 25°C
0.8
-
pH 7.6, 37°C, mutant enzyme D123N
0.8
-
pH 7.6, 37°C, mutant enzyme D125A
1.53
-
mutant R347A, pH 7.6, 37°C
1.53
-
pH 7.6, 37°C, mutant enzyme R347
1.55
-
mutant D374A, pH 7.6, 37°C
1.55
-
pH 7.6, 37°C, mutant enzyme D374A
1.73
-
pH 7.6, 55°C, peptidylarginine deiminase 3
1.8
-
mutant D169A, pH 7.6, 37°C
1.8
-
mutant F221A/F222A, pH 7.6, 37°C
1.8
-
pH 7.6, 37°C, mutant enzyme D169A
1.8
-
pH 7.6, 37°C, mutant enzyme F221A/F222A
2.3
-
mutant R441A, pH 7.5, 25°C
2.65
-
mutant D177A, pH 7.6, 37°C
2.65
-
pH 7.6, 37°C, mutant enzyme D177A
2.65
-
pH 7.6, 37°C, wild-type enzyme
2.65
-
wild-type, pH 7.6, 37°C
2.8
-
mutant Y435A, pH 7.5, 25°C
2.9
-
mutant V284D, pH 7.5, 25°C
3.3
-
mutant R8E/D547E, pH 7.4, 25°C
3.5
-
mutant D465A, pH 7.5, 25°C
3.6
-
mutant L279D, pH 7.5, 25°C
3.7
-
mutant R374Q, pH 7.5, 25°C
4
-
mutant Y435N, pH 7.4, 25°C
4.5
-
mutant L6D, pH 7.5, 25°C
5
-
mutant R639A, pH 7.5, 25°C
5.3
-
mutant R8L, pH 7.4, 25°C
5.5
-
mutant L279A, pH 7.5, 25°C
5.5
-
mutant V283T, pH 7.5, 25°C
5.5
-
mutant V284A, pH 7.5, 25°C
5.9
-
mutant Y435A, pH 7.4, 25°C
5.94
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
6.2
-
mutant W548F, pH 7.5, 25°C
6.9
-
mutant F285A, pH 7.5, 25°C
7.3
-
mutant L6A, pH 7.5, 25°C
7.3
-
mutant R8E, pH 7.4, 25°C
7.7
-
mutant F541A, pH 7.5, 25°C
7.8
-
mutant R374A, pH 7.5, 25°C
8
-
mutant C434A, pH 7.5, 25°C
8
-
mutant V283A, pH 7.5, 25°C
8.9
-
mutant D547E, pH 7.4, 25°C
9.5
-
mutant V283I, pH 7.5, 25°C
9.8
-
mutant F576A, pH 7.5, 25°C
10.08
-
mutant R8K, pH 7.4, 25°C
10.7
-
recombinant enzyme
10.7
-
mutant R8A/D547A, pH 7.4, 25°C
10.9
-
mutant L6I, pH 7.5, 25°C
10.9
-
mutant V284I, pH 7.5, 25°C
11.2
-
mutant L279I, pH 7.5, 25°C
11.31
-
pH 7.6, 55°C, peptidylarginine deiminase 1
11.6
-
mutant D547A, pH 7.4, 25°C
11.7
-
wild-type, pH 7.5, 25°C
12.1
-
mutant E281A, pH 7.4, 25°C
12.2
-
mutant D547N, pH 7.4, 25°C
12.2
-
mutant R8A, pH 7.4, 25°C
12.2
-
mutant R8Q , pH 7.4, 25°C
13.2
-
mutant Y237A/E281A, pH 7.4, 25°C
13.3
-
mutant R8H, pH 7.4, 25°C
13.4
-
wild-type, pH 7.4, 25°C
13.5
-
mutant D273A/R544A, pH 7.4, 25°C
13.9
-
mutant Y237A, pH 7.4, 25°C
15.24
-
pH 7.6, 55°C, peptidylarginine deiminase 2
0.019
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
0.03
-
pH 7.6, 37°C, mutant enzyme Q350A
0.1
-
pH 7.6, 37°C, mutant enzyme E412A
0.2
-
pH 7.6, 37°C, mutant enzyme W373A
0.25
-
pH 7.6, 37°C, mutant enzyme E352A
0.35
-
pH 7.6, 37°C, mutant enzyme D166A
0.51
-
pH 7.6, 37°C, mutant enzyme D389A
0.6
-
pH 7.6, 37°C, mutant enzyme D370A
0.8
-
pH 7.6, 37°C, mutant enzyme D123N
0.8
-
pH 7.6, 37°C, mutant enzyme D125A
1.53
-
pH 7.6, 37°C, mutant enzyme R347
1.55
-
pH 7.6, 37°C, mutant enzyme D374A
1.8
-
pH 7.6, 37°C, mutant enzyme D169A
1.8
-
pH 7.6, 37°C, mutant enzyme F221A/F222A
2.65
-
pH 7.6, 37°C, mutant enzyme D177A
2.65
-
pH 7.6, 37°C, wild-type enzyme
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0.08
-
Cbeta-kallikrein, pH 8.0, 25°C
0.109
-
Abeta-kallikrein, pH 8.0, 25°C
0.234
-
alpha-kallikrein, pH 8.0, 25°C
0.333
-
Tbeta-kallikrein, pH 8.0, 25°C
0.014
-
pH 8.0, 25°C, isoenzyme aT-II
0.031
-
pH 8.0, 25°C, isoenzyme aT-I
1.26
-
in 20 mM TBS (pH 7.6) for 10 min at 25°C, in the absence of sugars or glycoproteins
2.81
-
in 20 mM TBS (pH 7.6) for 10 min at 25°C, in the presence of 0.2 M methyl-alpha-D-galactoside
3.2
-
in 20 mM TBS (pH 7.6) for 10 min at 25°C, in the presence of 0.2 M methyl-alpha-D-mannoside
32
-
enzyme with O-carboxymethyl-poly-beta-cyclodextrin attached to surface, pH 8.0, 25°C
35.5
-
wild-type, pH 8.0, 25°C
7
-
subtilisin Novo, subtilisin Carlsberg
89
-
pH 5.6, 25°C, in 0.3 M KCl
200
-
enzyme form SB2, benzoyl-Gly ethyl ester, enzyme form SB1 and SB2
0.24
0.25
depending on assay method
0.1
-
mutant F221A/F222A, pH 7.6, 37°C
0.1
-
mutant V469T, pH 7.5, 25°C
0.1
-
pH 7.6, 37°C, mutant enzyme F221A/F222A
0.12
-
mutant D123N, pH 7.6, 37°C
0.12
-
pH 7.6, 37°C, mutant enzyme D123N
0.14
-
mutant D125A, pH 7.6, 37°C
0.14
-
pH 7.6, 37°C, mutant enzyme D125A
0.15
-
pH 7.6, 37°C, hPADI2 expressed by baculovirus
0.16
-
pH 7.6, 37°C, wild-type enzyme
0.16
-
wild-type, pH 7.6, 37°C
0.19
-
isozyme PAD1, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
0.25
-
mutant D169A, pH 7.6, 37°C
0.25
-
pH 7.6, 37°C, mutant enzyme D169A
0.27
-
at pH 7.6 and 37°C
0.3
-
mutant W548K, pH 7.5, 25°C
0.31
-
wild-type, pH 7.4, 25°C
0.33
-
mutant D166A, pH 7.6, 37°C
0.33
-
pH 7.6, 37°C, mutant enzyme D166A
0.35
-
pH 7.6, 55°C, peptidylarginine deiminase 1
0.35
-
mutant D273A/R544A, pH 7.4, 25°C
0.36
-
mutant D547A, pH 7.4, 25°C
0.36
-
mutant Y237A, pH 7.4, 25°C
0.38
-
mutant Y237A/E281A, pH 7.4, 25°C
0.4
-
mutant C434A, pH 7.5, 25°C
0.4
-
mutant D465A, pH 7.5, 25°C
0.4
-
mutant F576A, pH 7.5, 25°C
0.4
-
mutant L279A, pH 7.5, 25°C
0.4
-
mutant L279I, pH 7.5, 25°C
0.4
-
mutant R374Q, pH 7.5, 25°C
0.4
-
mutant R8A/D547A, pH 7.4, 25°C
0.45
-
mutant E281A, pH 7.4, 25°C
0.47
-
mutant R8A, pH 7.4, 25°C
0.47
-
mutant R8H, pH 7.4, 25°C
0.5
-
pH 7.6, 55°C, peptidylarginine deiminase 2
0.5
-
mutant L6D, pH 7.5, 25°C
0.5
-
mutant L6I, pH 7.5, 25°C
0.5
-
mutant V283I, pH 7.5, 25°C
0.5
-
mutant V284I, pH 7.5, 25°C
0.5
-
wild-type, pH 7.5, 25°C
0.5
-
mutant R8K, pH 7.4, 25°C
0.54
-
recombinant enzyme
0.6
-
mutant D389A, pH 7.6, 37°C
0.6
-
mutant L6A, pH 7.5, 25°C
0.6
-
pH 7.6, 37°C, mutant enzyme D389A
0.6
-
mutant R8Q , pH 7.4, 25°C
0.7
-
mutant F541A, pH 7.5, 25°C
0.7
-
mutant R374A, pH 7.5, 25°C
0.7
-
mutant R639A, pH 7.5, 25°C
0.7
-
mutant V283A, pH 7.5, 25°C
0.72
-
mutant D547E, pH 7.4, 25°C
0.73
-
pH 7.6, 37°C, hPADI2 expressed in Escherichia coli
0.78
-
Km-value of the high activity binding site
0.8
-
mutant F285A, pH 7.5, 25°C
0.86
-
mutant D547N, pH 7.4, 25°C
0.9
-
mutant V283T, pH 7.5, 25°C
0.9
-
mutant V284D, pH 7.5, 25°C
0.91
-
pH 7.6, 37°C, hPADI4 expressed in Escherichia coli
1
-
mutant V469L, pH 7.5, 25°C
1.06
-
mutant R8E, pH 7.4, 25°C
1.36
-
isozyme PAD4, at 37°C, 10 mM CaCl2, 50 mM NaCl, 100 mM Tris-HCl, pH 7.6, 2 mM dithiothreitol
1.36
-
at pH 7.5 and 37°C
1.36
-
mutant R8L, pH 7.4, 25°C
1.4
-
mutant W548F, pH 7.5, 25°C
1.5
-
mutant V284A, pH 7.5, 25°C
1.7
-
mutant R441A, pH 7.5, 25°C
1.9
-
mutant L279D, pH 7.5, 25°C
2.3
-
mutant R372Q, pH 7.5, 25°C
2.33
-
mutant Y435A, pH 7.4, 25°C
2.4
-
mutant D177A, pH 7.6, 37°C
2.4
-
pH 7.6, 37°C, mutant enzyme D177A
2.73
-
mutant Y435N, pH 7.4, 25°C
2.77
-
mutant R8E/D547E, pH 7.4, 25°C
3.2
-
mutant Y435A, pH 7.5, 25°C
3.4
-
mutant E352A, pH 7.6, 37°C
3.4
-
pH 7.6, 37°C, mutant enzyme E352A
3.7
-
mutant R372A, pH 7.5, 25°C
4.4
-
mutant R347A, pH 7.6, 37°C
4.4
-
pH 7.6, 37°C, mutant enzyme R347
5
-
mutant D370A, pH 7.6, 37°C
5
-
pH 7.6, 37°C, mutant enzyme D370A
5.3
-
mutant V469A, pH 7.5, 25°C
6.3
-
mutant Q350A, pH 7.6, 37°C
6.3
-
pH 7.6, 37°C, mutant enzyme Q350A
7.5
-
pH 7.6, 55°C, peptidylarginine deiminase 3
8
-
mutant D374A, pH 7.6, 37°C
8
-
pH 7.6, 37°C, mutant enzyme D374A
11.2
-
Km-value of the low activity binding site
13
-
mutant E412A, pH 7.6, 37°C
13
-
pH 7.6, 37°C, mutant enzyme E412A
30
-
mutant R373A, pH 7.6, 37°C
30
-
pH 7.6, 37°C, mutant enzyme W373A
0.1
-
pH 7.6, 37°C, mutant enzyme F221A/F222A
0.12
-
pH 7.6, 37°C, mutant enzyme D123N
0.14
-
pH 7.6, 37°C, mutant enzyme D125A
0.16
-
pH 7.6, 37°C, wild-type enzyme
0.25
-
pH 7.6, 37°C, mutant enzyme D169A
0.33
-
pH 7.6, 37°C, mutant enzyme D166A
0.6
-
pH 7.6, 37°C, mutant enzyme D389A
2.4
-
pH 7.6, 37°C, mutant enzyme D177A
3.4
-
pH 7.6, 37°C, mutant enzyme E352A
4.4
-
pH 7.6, 37°C, mutant enzyme R347
5
-
pH 7.6, 37°C, mutant enzyme D370A
6.3
-
pH 7.6, 37°C, mutant enzyme Q350A
8
-
pH 7.6, 37°C, mutant enzyme D374A
13
-
pH 7.6, 37°C, mutant enzyme E412A
18
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C
30
-
pH 7.6, 37°C, mutant enzyme W373A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Afaacytin, an alpha beta-fibrinogenase from Cerastes cerastes (horned viper) venom, activates purified factor X and induces serotonin release from human blood platelets
1995
Laraba-Diebari, F.; Martin-Eauclaire, M.F.; Mauco, G.; Marchot, P.
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756-765
Tryptase from rat skin: purification and properties
1991
Braganza, V.J.; Simmons, W.H.
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4997-5007
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The subtilisins
1970
Ottesen, M.; Svendsen, I.
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Subtilisins: primary structure, chemical and physical properties
1971
Markland, F.S.; Smith, E.L.
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
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561-608
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The properties of subtilisin, novo type, immobilized on porous glass
1995
Trzmiel, T.; Fortak, M.; Galas, E.
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Isolation of alkaline proteinases from Aspergillus oryzae by one-step affinity chromatography on ovoinhibitor-sepharose column
1973
Feinstein, G.; Gertler, A.
Biochim. Biophys. Acta
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196-202
Alkaline protease from Aspergillus oryzae: esterase activity
1972
Ku, H.C.; Wyborny, L.; Kalnitsky, G.
Biochim. Biophys. Acta
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225-232
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Specificity of proteinase K from Tritirachium album Limber for synthetic peptides
1975
Morihara, K.; Tsuzuki, H.
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1489-1492
The coagulant enzyme from Bothrops atrox venom (batroxobin)
1976
Stocker, K.; Barlow, G.H.
Methods Enzymol.
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Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom
1976
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205-213
Protease II from Escherichia coli. Purification and characterization
1975
Pacaud, M.; Richaud, C.
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7771-7779
Oligopeptidase B: protease II from Escherichia coli
1994
Tsuru, D.; Yoshimoto, T.
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Protease II from Escherichia coli. Substrate specificity and kinetic properties
1978
Pacaud, M.
Eur. J. Biochem.
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Snake venom proteases that activate blood-coagulation factor V
1981
Kisiel, W.; Canfield, W.M.
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275-285
Isolation of highly active papaya peptidases A and B from commercial chymopapain
1981
Polgar, L.
Biochim. Biophys. Acta
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262-269
Characterization of papaya peptidase A as a cysteine proteinase of Carica papaya L. with active-centre properties that differ from those of papain by using 2,2-dipyridyl disulphide and 4-chloro-7-nitrobenzofurazan as reactivity probes. Use of two-protonic-state electrophiles in the identification of catalytic-site thiol groups
1982
Baines, B.S.; Brocklehurst, K.
Biochem. J.
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205-211
Isolation and characterization of papaya peptidase A from commercial chymopapain
1975
Robinson, G.W.
Biochemistry
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3695-3700
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Bromelain enzymes
1970
Murachi, T.
Methods Enzymol.
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273-284
Bromelain enzymes
1976
Murachi, T.
Methods Enzymol.
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475-485
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Fractionation, purification, and some properties of proteolytic enzymes from stem bromelain
1971
Minami, Y.; Doi, E.; Hata, T.
Agric. Biol. Chem.
35
1419-1430
Multiple molecular forms of stem bromelain. Isolation and characterization of two closely related components, SB1 and SB2
1973
Takahashi, N.; Yasuda, Y.; Goto, K.; Miyake, T.; Murachi, T.
J. Biochem.
74
355-373
Purification and characterization of a proteinase from pineapple fruit, fruit bromelain FA2
1976
Yamada, F.; Takahashi, N.; Murachi, T.
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1223-1234
Studies on ram acrosin. Isolation from spermatozoa, activation by cations and organic solvents, and influence of cations on its reaction with inhibitors
1975
Brown, C.R.; Andani, Z.; Hartree, E.F.
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133-146
Caprine acrosin. Purification, characterization and proteolysis of the porcine zona pellucida
1989
Hardy, D.M.; Schoots, A.F.M.; Hedrick, J.L.
Biochem. J.
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Characterization of mouse epididymal acrosin: comparative studies with acrosin from boar and human ejaculated spermatozoa
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Int. J. Androl.
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95-104
Bovine epididymal sperm proacrosin-acrosin system: quantification and partial characterization
1992
NagDas, S.K.
Andrologia
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Human factor D of the alternative complement pathway: purification and characterization
1977
Volanakis, J.E.; Schrohenloher, R.E.; Stroud, R.M.
J. Immunol.
119
337-342
Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. specificity and inhibition studies of Achromobacter protease I
1981
Masaki, T.; Fujihashi, T.; Nakamura, K.; Soejima, M.
Biochim. Biophys. Acta
660
51-55
-
A new proteolytic enzyme from Achromobacter lyticus M497-1
1978
Masaki, T.; Nakamura, T.; Isono, M.; Soejima, M.
Agric. Biol. Chem.
42
1443-1445
-
Cathepsins
1970
Mycek, M.J.
Methods Enzymol.
19
285-315
Crystallization and properties of cathepsin B from rat liver
1979
Towatari, T.; Kawabata, Y.; Katunuma, N.
Eur. J. Biochem.
102
279-289
Isolation and characterization of three forms of cathepsin B from porcine liver
1979
Takahashi, K.; Isemura, M.; Ikenaka, R.
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85
1053-1060
Human placental cathepsin B1. Isolation and some physical properties
1974
Swanson, A.A.; Martin, B.J.; Spicer, S.S.
Biochem. J.
137
223-228
Leucostoma peptidase A
1976
Prescott, J.M.; Wagner, F.W.
Methods Enzymol.
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397-404
The human complement system serine proteases C1bar and C1sbar and their proenzymes
1981
Sim, R.B.
Methods Enzymol.
80
26-42
Human complement serine proteases C1r and C1s and their proenzymes
1993
Arlaud, G.J.; Thielens, N.M.
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223
61-82
The specificity of actinidin and its relationship to the structure of the enzyme
1980
Baker, E.N.; Boland, M.J.; Calder, P.C.; Hardman, M.J.
Biochim. Biophys. Acta
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30-34
Kinetic studies on the thiol protease from Actinidia chinensis
1972
Boland, M.J.; Hardman, M.J.
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The peptidylarginine deiminases expressed in human epidermis differ in their substrate specificities and subcellular locations
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Preparation and characterization of a truncated caricain lacking 41 residues from the N-terminal
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Preparation and characterisation of spray-dried and crystallised trypsin: FT-Raman study to detect protein denaturation after thermal stress
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Effect of PEG molecular weight and linking chemistry on the biological activity and thermal stability of PEGylated trypsin
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Expression of peptidylarginine deiminase from Porphyromonas gingivalis in Escherichia coli: enzyme purification and characterization
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Substrate specificity and kinetic studies of PADs 1, 3, and 4 identify potent and selective inhibitors of protein arginine deiminase 3
2010
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Biochemistry
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Characterization and inactivation of an agmatine deiminase from Helicobacter pylori
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Purification and characterization of trypsin from the pyloric ceca of orange-spotted grouper, Epinephelus coioides
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Investigation of the structure and proteolytic activity of papain inaqueous miscible organic media
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Vacuolating, lethal, collagenase and clostripain activities of six reference ATCC Clostridium histolyticum strains
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Arginine metabolising enzymes as therapeutic tools for Alzheimers disease: peptidyl arginine deiminase catalyses fibrillogenesis of beta-amyloid peptides
2010
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Mol. Neurobiol.
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Functional role of dimerization of human peptidylarginine deiminase 4 (PAD4)
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Studies on the regioselectivity and kinetics of the action of trypsin on proinsulin and its derivatives using mass spectrometry
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Porphyromonas gingivalis peptidylarginine deiminase substrate specificity
2013
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Anaerobe
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Mechanistic studies of protein arginine deiminase 2: evidence for a substrate-assisted mechanism
2014
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Biochemistry
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Novel small molecule protein arginine deiminase 4 (PAD4) inhibitors
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Comp. Biochem. Physiol. B
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Protein arginine deiminase 2 binds calcium in an ordered fashion implications for inhibitor design
2015
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Crystal structure of Porphyromonas gingivalis peptidylarginine deiminase implications for autoimmunity in rheumatoid arthritis
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Novel furan-containing peptide-based inhibitors of protein arginine deiminase type IV (PAD4)
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Molecular interplay between the dimer interface and the substrate-binding site of human peptidylarginine deiminase 4
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