BRENDA - Enzyme Database
show all sequences of 3.4.17.3

Some properties of porcine carboxypeptidase N

Juillerat-Jeanneret, L.; Roth, M.; Bargetzi, J.P.; Hoppe-Seyler's Z. Physiol. Chem. 363, 51-58 (1982)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
4-aminomethyl-cyclohexane carboxylic acid
with benzoyl-Gly-Lys as substrate
Sus scrofa
6-aminohexanoic acid
with benzoyl-Gly-Lys or hippuryl-argininic acid as substrate
Sus scrofa
Arg
D-Arg; L-Arg; with benzoyl-Gly-Lys or hippuryl-argininic acid as substrate
Sus scrofa
Argininic acid
inhibition of peptidase activity and esterase activity; with benzoyl-Gly-Lys, hippuryl-argininic acid or with benzoyl-Gly-Arg as substrate
Sus scrofa
benzoyl-L-Arg
with benzoyl-Gly-Arg as substrate
Sus scrofa
Benzyloxycarbonyl-Arg
with benzoyl-Gly-Arg as substrate
Sus scrofa
hippuric acid
with benzoyl-Gly-Arg as substrate
Sus scrofa
Hippuryl-L-argininic acid
with benzoyl-Gly-Arg as substrate
Sus scrofa
Lys
with hippuryl-argininic acid as substrate
Sus scrofa
Nalpha-acetyl-Arg
with benzoyl-Gly-Lys or benzoyl-Gly-Arg as substrate
Sus scrofa
Nalpha-acetyl-Lys
with benzoyl-Gly-Lys as substrate
Sus scrofa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
5.9
-
Leu-Trp-Met-Arg
-
Sus scrofa
6.3
-
Benzoyl-Gly-Lys
-
Sus scrofa
6.7
-
benzoyl-Gly-Arg
-
Sus scrofa
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
metalloenzyme, methyl is tightly bound to the apoenzyme at neutral pH
Sus scrofa
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
315000
-
-
Sus scrofa
Organism
Organism
UniProt
Commentary
Textmining
Sus scrofa
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
additional information
-
-
Sus scrofa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
-
36405
Sus scrofa
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
-
-
?
benzoyl-Gly-Arg + H2O
-
36405
Sus scrofa
benzoyl-Gly + Arg
-
36405
Sus scrofa
?
benzoyl-Gly-argininic acid + H2O
-
36405
Sus scrofa
benzoyl-Gly + argininic acid
-
36405
Sus scrofa
?
benzoyl-Gly-Lys + H2O
-
36405
Sus scrofa
benzoyl-Gly + Lys
-
36405
Sus scrofa
?
benzyloxycarbonyl-Val-Gly-Lys-Lys + H2O
-
36405
Sus scrofa
Lys + benzyloxycarbonyl-Val-Gly-Lys
-
36405
Sus scrofa
?
fibrinopeptide A + H2O
very low activity
36405
Sus scrofa
Arg + ?
-
36405
Sus scrofa
?
fibrinopeptide B + H2O
-
36405
Sus scrofa
Arg + ?
-
36405
Sus scrofa
?
Gly-His-Lys + H2O
-
36405
Sus scrofa
Gly-His + Lys
-
36405
Sus scrofa
?
Hippuryl-L-Lys + H2O
-
36405
Sus scrofa
Hippuric acid + L-Lys
-
-
-
?
Leu-Trp-Met-Arg + H2O
-
36405
Sus scrofa
Leu-Trp-Met + Arg
-
36405
Sus scrofa
?
polylysine + H2O
-
36405
Sus scrofa
Lys
-
36405
Sus scrofa
?
Pro-Gly-Lys-Ala-Arg + H2O
-
36405
Sus scrofa
Pro-Gly-Lys-Ala + Arg
-
36405
Sus scrofa
?
Pro-Phe-Gly-Lys + H2O
-
36405
Sus scrofa
Pro-Phe-Gly + Lys
-
36405
Sus scrofa
?
salmine + H2O
-
36405
Sus scrofa
Arg + ?
-
36405
Sus scrofa
?
Thr-Pro-Arg-Lys + H2O
-
36405
Sus scrofa
Thr-Pro-Arg + Lys
-
36405
Sus scrofa
?
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
4-aminomethyl-cyclohexane carboxylic acid
with benzoyl-Gly-Lys as substrate
Sus scrofa
6-aminohexanoic acid
with benzoyl-Gly-Lys or hippuryl-argininic acid as substrate
Sus scrofa
Arg
L-Arg
Sus scrofa
Arg
with benzoyl-Gly-Lys or hippuryl-argininic acid as substrate
Sus scrofa
Arg
D-Arg
Sus scrofa
Argininic acid
with benzoyl-Gly-Lys, hippuryl-argininic acid or with benzoyl-Gly-Arg as substrate
Sus scrofa
Argininic acid
inhibition of peptidase activity and esterase activity
Sus scrofa
benzoyl-L-Arg
with benzoyl-Gly-Arg as substrate
Sus scrofa
Benzyloxycarbonyl-Arg
with benzoyl-Gly-Arg as substrate
Sus scrofa
hippuric acid
with benzoyl-Gly-Arg as substrate
Sus scrofa
Hippuryl-L-argininic acid
with benzoyl-Gly-Arg as substrate
Sus scrofa
Lys
with hippuryl-argininic acid as substrate
Sus scrofa
Nalpha-acetyl-Arg
with benzoyl-Gly-Lys or benzoyl-Gly-Arg as substrate
Sus scrofa
Nalpha-acetyl-Lys
with benzoyl-Gly-Lys as substrate
Sus scrofa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
5.9
-
Leu-Trp-Met-Arg
-
Sus scrofa
6.3
-
Benzoyl-Gly-Lys
-
Sus scrofa
6.7
-
benzoyl-Gly-Arg
-
Sus scrofa
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
metalloenzyme, methyl is tightly bound to the apoenzyme at neutral pH
Sus scrofa
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
315000
-
-
Sus scrofa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
additional information
-
-
Sus scrofa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
-
36405
Sus scrofa
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
-
-
?
benzoyl-Gly-Arg + H2O
-
36405
Sus scrofa
benzoyl-Gly + Arg
-
36405
Sus scrofa
?
benzoyl-Gly-argininic acid + H2O
-
36405
Sus scrofa
benzoyl-Gly + argininic acid
-
36405
Sus scrofa
?
benzoyl-Gly-Lys + H2O
-
36405
Sus scrofa
benzoyl-Gly + Lys
-
36405
Sus scrofa
?
benzyloxycarbonyl-Val-Gly-Lys-Lys + H2O
-
36405
Sus scrofa
Lys + benzyloxycarbonyl-Val-Gly-Lys
-
36405
Sus scrofa
?
fibrinopeptide A + H2O
very low activity
36405
Sus scrofa
Arg + ?
-
36405
Sus scrofa
?
fibrinopeptide B + H2O
-
36405
Sus scrofa
Arg + ?
-
36405
Sus scrofa
?
Gly-His-Lys + H2O
-
36405
Sus scrofa
Gly-His + Lys
-
36405
Sus scrofa
?
Hippuryl-L-Lys + H2O
-
36405
Sus scrofa
Hippuric acid + L-Lys
-
-
-
?
Leu-Trp-Met-Arg + H2O
-
36405
Sus scrofa
Leu-Trp-Met + Arg
-
36405
Sus scrofa
?
polylysine + H2O
-
36405
Sus scrofa
Lys
-
36405
Sus scrofa
?
Pro-Gly-Lys-Ala-Arg + H2O
-
36405
Sus scrofa
Pro-Gly-Lys-Ala + Arg
-
36405
Sus scrofa
?
Pro-Phe-Gly-Lys + H2O
-
36405
Sus scrofa
Pro-Phe-Gly + Lys
-
36405
Sus scrofa
?
salmine + H2O
-
36405
Sus scrofa
Arg + ?
-
36405
Sus scrofa
?
Thr-Pro-Arg-Lys + H2O
-
36405
Sus scrofa
Thr-Pro-Arg + Lys
-
36405
Sus scrofa
?
Other publictions for EC 3.4.17.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [░C]
Temperature Range [░C]
Temperature Stability [░C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [░C] (protein specific)
Temperature Range [░C] (protein specific)
Temperature Stability [░C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
754517
Leung
Carboxypeptidase B2 and carbo ...
Mus musculus
J. Thromb. Haemost.
16
1474-1486
2018
-
-
-
-
-
-
2
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
4
4
-
-
-
755462
Wu
Fine-tune regulation of carbo ...
Danio rerio
Sci. Rep.
7
1852
2017
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
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-
2
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-
2
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2
-
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-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
731670
Li
Circulating proteolytic produc ...
Mus musculus
Clin. Chem.
60
233-242
2014
-
-
-
-
-
-
-
-
-
-
-
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-
1
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1
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1
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2
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-
1
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
732362
Helwig
Photoperiod-dependent regulati ...
Phodopus sungorus
J. Neuroendocrinol.
25
190-197
2013
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
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-
-
1
1
-
1
-
1
1
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-
1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
1
-
-
-
1
-
-
-
1
-
-
1
-
-
731248
Talens
Binding of carboxypeptidase N ...
Homo sapiens
Biochem. Biophys. Res. Commun.
427
421-425
2012
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
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1
-
2
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1
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
698988
Du
Regulation of chemerin bioacti ...
Homo sapiens
J. Biol. Chem.
284
751-758
2009
1
-
-
-
-
-
1
23
-
-
-
-
-
2
-
-
-
-
-
4
-
-
27
-
7
3
-
-
23
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
23
-
-
-
-
-
-
-
-
-
4
-
-
27
-
3
-
-
23
-
-
-
-
-
-
-
-
-
-
695421
Leung
Regulation of tissue inflammat ...
Mus musculus
Adv. Exp. Med. Biol.
632
61-69
2008
1
1
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
1
-
-
1
-
8
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
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-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
700246
Leung
Regulation of tissue inflammat ...
Mus musculus
Mol. Immunol.
45
4080-4083
2008
1
1
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
1
-
-
5
-
8
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668070
Davis
Identification of carboxypepti ...
Homo sapiens
Blood
105
4561-4568
2005
-
-
-
-
-
-
-
-
1
-
-
1
-
3
-
-
1
-
-
3
2
-
2
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
1
-
3
2
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
653008
Suzuki
Enhancement of fibrinolysis by ...
Homo sapiens, Rattus norvegicus
J. Pharmacol. Exp. Ther.
309
607-615
2004
-
-
-
-
-
-
2
-
2
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
2
2
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668371
Matthews
Expression of the third comple ...
Mus musculus
Dev. Comp. Immunol.
28
647-655
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670291
Matthews
Carboxypeptidase N: a pleiotro ...
Homo sapiens, Mus musculus
Mol. Immunol.
40
785-793
2004
1
-
2
-
-
-
1
-
3
2
2
2
-
2
-
-
-
-
-
10
-
-
4
4
4
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
1
-
-
3
2
2
2
-
-
-
-
-
10
-
-
4
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
650827
Lazoura
Rational structure-based desig ...
Homo sapiens
Chem. Biol.
9
1129-1139
2002
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
2
-
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-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
653144
Campbell
Inactivation of C3a and C5a oc ...
Homo sapiens
Microbiol. Immunol.
46
131-134
2002
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
4
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
653145
Komura
Heat stability of carboxypepti ...
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Microbiol. Immunol.
46
217-223
2002
-
-
-
-
-
-
-
-
-
-
-
-
-
16
-
-
-
-
-
4
-
-
8
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
8
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
652673
Sato
Pro-carboxypeptidase R is an a ...
Mus musculus
J. Immunol.
165
1053-1058
2000
-
-
1
-
-
-
1
-
-
-
-
2
-
9
-
-
-
-
-
2
-
-
4
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
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36414
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Skidgel
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36417
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Ryan
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36403
Grimwood
Characterization of the carbox ...
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36402
Hendriks
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Carboxypeptidase N activity in ...
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Hendriks
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36394
Skidgel
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Carboxypeptidase N (arginine c ...
Homo sapiens
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
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1984
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Schweisfurth
Carboxypeptidase N ...
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1984
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36397
Fricker
Enkephalin convertase: potent, ...
Homo sapiens
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1983
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36399
Levin
Isolation and characterization ...
Homo sapiens
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1982
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Juillerat-Jeanneret
Some properties of porcine car ...
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36395
Plummer
Human plasma carboxypeptidase ...
Homo sapiens
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1981
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Plummer
An improved spectrophotometric ...
Homo sapiens
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36410
Erd÷s
Inhibitors of kininases ...
Homo sapiens
Fed. Proc.
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1979
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3
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1
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36396
Plummer
Human plasma carboxypeptidase ...
Homo sapiens
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1
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1
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5
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5
1
1
1
1
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36411
Koheil
Isoelectric focusing of carbox ...
Homo sapiens
Biochim. Biophys. Acta
524
156-161
1978
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36404
Jeanneret
Carboxypeptidase N from pig se ...
Sus scrofa
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357
867-872
1976
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7
3
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1
3
1
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3
1
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36400
Oshima
Plasma carboxypeptidase N, sub ...
Homo sapiens
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170
132-138
1975
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11
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11
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36401
Oshima
-
Subunits of human plasma carbo ...
Homo sapiens, Sus scrofa
Biochim. Biophys. Acta
365
344-348
1974
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4
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2
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3
1
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2
2
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