Cloned (Comment) | Organism |
---|---|
mouse | Mus musculus |
mouse | Homo sapiens |
mouse | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1,10-phenanthroline | - |
Homo sapiens | |
1,10-phenanthroline | - |
Mus musculus | |
1,10-phenanthroline | - |
Rattus norvegicus | |
2-mercaptoethanol | - |
Homo sapiens | |
2-mercaptoethanol | - |
Mus musculus | |
2-mercaptoethanol | - |
Rattus norvegicus | |
Acetyl-Arg-Pro-Gly-Tyr hydroxamate | kinetics | Mus musculus | |
actinonin | i.e. 3-[[1-[[2-(hydroxymethyl)-1-pyrolidinyl]carbonyl]-2-methylpropyl]carbamoyl]octano hydroxamic acid, strong, kinetics | Mus musculus | |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Glu-Pro-Phe-Arg | - |
Mus musculus | |
captopril | not | Homo sapiens | |
captopril | not | Mus musculus | |
captopril | not | Rattus norvegicus | |
cysteine | - |
Homo sapiens | |
cysteine | - |
Mus musculus | |
cysteine | - |
Rattus norvegicus | |
EDTA | reversed by Zn2+ | Homo sapiens | |
EDTA | reversed by Zn2+ | Mus musculus | |
EDTA | reversed by Zn2+ | Rattus norvegicus | |
Hydroxamyl-succinyl-Pro-Phe-Arg | kinetics | Mus musculus | |
additional information | 3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor | Homo sapiens | |
additional information | 3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor | Mus musculus | |
additional information | 3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.174 | - |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg | - |
Mus musculus | |
0.182 | - |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg | - |
Mus musculus | |
0.183 | - |
2-Aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
0.22 | - |
2-Aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
0.226 | - |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg | - |
Mus musculus | |
0.29 | - |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg | - |
Mus musculus | |
0.296 | - |
2-Aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
0.331 | - |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg | - |
Mus musculus | |
0.402 | - |
2-Aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
1.22 | - |
2-Aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
1.38 | - |
2-Aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
2.46 | - |
2-Aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Homo sapiens | 16020 | - |
membrane | renal brush border membrane | Mus musculus | 16020 | - |
membrane | renal brush border membrane | Rattus norvegicus | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Calcium | metalloendopeptidase | Mus musculus | |
Calcium | metalloendopeptidase | Homo sapiens | |
Calcium | metalloendopeptidase | Rattus norvegicus | |
Calcium | 3 mol calcium per mol subunit (atomic absorption spectroscopy) | Mus musculus | |
Calcium | 3 mol calcium per mol subunit (atomic absorption spectroscopy) | Homo sapiens | |
Calcium | 3 mol calcium per mol subunit (atomic absorption spectroscopy) | Rattus norvegicus | |
Calcium | Ca2+ reactivates inactive apoenzyme | Mus musculus | |
Calcium | Ca2+ reactivates inactive apoenzyme | Homo sapiens | |
Calcium | Ca2+ reactivates inactive apoenzyme | Rattus norvegicus | |
additional information | Cu2+ does not reactivate inactive apoenzyme | Mus musculus | |
additional information | Cu2+ does not reactivate inactive apoenzyme | Homo sapiens | |
additional information | Cu2+ does not reactivate inactive apoenzyme | Rattus norvegicus | |
Zinc | metalloendopeptidase | Mus musculus | |
Zinc | metalloendopeptidase | Homo sapiens | |
Zinc | metalloendopeptidase | Rattus norvegicus | |
Zinc | 1 mol zinc per mol subunit (atomic absorption spectroscopy) | Mus musculus | |
Zinc | zinc binding motif | Mus musculus | |
Zinc | zinc binding motif | Homo sapiens | |
Zinc | zinc binding motif | Rattus norvegicus | |
Zinc | Zn2+ reactivates inactive apoenzyme | Mus musculus | |
Zinc | Zn2+ reactivates inactive apoenzyme | Homo sapiens | |
Zinc | Zn2+ reactivates inactive apoenzyme | Rattus norvegicus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Homo sapiens |
additional information | - |
amino acid sequence, domain structure and tertiary structure deduced from cDNAs | Mus musculus |
additional information | - |
amino acid sequence, domain structure and tertiary structure deduced from cDNAs | Rattus norvegicus |
85000 | - |
4 * 85000, mouse | Mus musculus |
85000 | - |
4 * 85000, mouse | Rattus norvegicus |
90000 | - |
x * 90000, mouse, SDS-PAGE, reducing conditions | Mus musculus |
90000 | - |
x * 90000, mouse, SDS-PAGE, reducing conditions | Rattus norvegicus |
270000 | 320000 | mouse, gel filtration | Mus musculus |
320000 | - |
mouse, gel filtration, SDS-PAGE in the absence of 2-mercaptoethanol | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
PPH | - |
Homo sapiens PPH | - |
PPH | - |
Mus musculus | - |
random bred ICR and at least 35 inbred, recombinant and congenic strains | - |
Rattus norvegicus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | no sialic acid | Mus musculus |
glycoprotein | no sialic acid | Homo sapiens |
glycoprotein | no sialic acid | Rattus norvegicus |
Purification (Comment) | Organism |
---|---|
- |
Mus musculus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
3.25-13 mg azocasein/min/mg | Mus musculus |
additional information | - |
3.25-13 mg azocasein/min/mg | Homo sapiens |
additional information | - |
3.25-13 mg azocasein/min/mg | Rattus norvegicus |
Storage Stability | Organism |
---|---|
-20°C, 1 mg enzyme/ml, more than a year with little loss of activity | Mus musculus |
4°C, 1 mg enzyme/ml at least 2 weeks with little loss of activity | Mus musculus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O | fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser | Mus musculus | 2-aminobenzoyl-Arg-Gly-Pro-Phe + Ser-Pro-(4-nitro)Phe-Arg | - |
? | |
2-aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O | fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser | Mus musculus | 2-aminobenzoyl-Arg-Hyp-Gly-Phe + Ser-Pro-(4-nitro)Phe-Arg | - |
? | |
2-aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg + H2O | fluorogenic bradykinin analog substrate, cleavage site: Ala-Ser | Mus musculus | 2-aminobenzoyl-Arg-Pro-Gly-Ala + Ser-Pro-(4-nitro)Phe-Arg | - |
? | |
2-aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-(4-nitro)Phe-Arg + H2O | fluorogenic bradykinin analog substrate, cleavage site: Glu-Ser | Mus musculus | 2-aminobenzoyl-Arg-Pro-Gly-Glu + Ser-Pro-(4-nitro)Phe-Arg | - |
? | |
2-aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg + H2O | fluorogenic bradykinin analog substrate, cleavage sites: Leu-Ser (major site) and Gly-Leu | Mus musculus | 2-aminobenzoyl-Arg-Pro-Gly-Leu + Ser-Pro-(4-nitro)Phe-Arg | major products | ? | |
2-aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg + H2O | fluorogenic bradykinin analog substrate, cleavage sites: Gly-Lys (major site) and Lys-Ser | Mus musculus | 2-aminobenzoyl-Arg-Pro-Gly + Lys-Ser-Pro-(4-nitro)Phe-Arg | major products | ? | |
2-aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O | fluorogenic bradykinin analog substrates, cleavage site: Phe-Ser | Mus musculus | 2-aminobenzoyl-Arg-Pro-Ile-Phe + Ser-Pro-(4-nitro)Phe-Arg | - |
? | |
alpha-melanocyte stimulating hormone + H2O | i.e. acetyl-Ser-Tyr-Ser-Met-Gly-His-Phe-Arg-Trp-Gly-Lys-Pro-Val, cleavage sites: Ser-Met, Gly-Lys, mouse | Mus musculus | ? | - |
? | |
angiotensin I + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleavage site: Tyr-Ile | Mus musculus | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu | - |
? | |
angiotensin I + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleavage site: Tyr-Ile | Homo sapiens | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu | - |
? | |
angiotensin I + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleavage site: Tyr-Ile | Rattus norvegicus | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu | - |
? | |
angiotensin II + H2O | cleavage site: Tyr-Ile | Mus musculus | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
angiotensin II + H2O | cleavage site: Tyr-Ile | Homo sapiens | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
angiotensin II + H2O | cleavage site: Tyr-Ile | Rattus norvegicus | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
angiotensin II + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe | Mus musculus | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
angiotensin II + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe | Homo sapiens | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
angiotensin II + H2O | i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe | Rattus norvegicus | Asp-Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
angiotensin III + H2O | i.e. Arg-Val-Tyr-Ile-His-Pro-Phe, cleavage site: Tyr-Ile | Mus musculus | Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
angiotensin III + H2O | i.e. Arg-Val-Tyr-Ile-His-Pro-Phe, cleavage site: Tyr-Ile | Homo sapiens | Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
angiotensin III + H2O | i.e. Arg-Val-Tyr-Ile-His-Pro-Phe, cleavage site: Tyr-Ile | Rattus norvegicus | Arg-Val-Tyr + Ile-His-Pro-Phe | - |
? | |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg + H2O | chromogenic bradykinin analog | Mus musculus | Arg-Pro-Pro-Gly-(4-nitro)Phe + Ala-Pro-Phe-Arg | - |
? | |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg + H2O | chromogenic bradykinin analog | Mus musculus | Arg-Pro-Pro-Gly-(4-nitro)Phe + Arg-Pro-Phe-Arg | - |
? | |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg + H2O | chromogenic bradykinin analog | Mus musculus | Arg-Pro-Pro-Gly-(4-nitro)Phe + Lys-Pro-Phe-Arg | - |
? | |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg + H2O | chromogenic bradykinin analog | Mus musculus | Arg-Pro-Pro-Gly-(4-nitro)Phe + Phe-Pro-Phe-Arg | - |
? | |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg + H2O | i.e. nitrobradykinin, chromogenic bradykinin analog | Mus musculus | Arg-Pro-Pro-Gly-(4-nitro)Phe + Ser-Pro-Phe-Arg | - |
? | |
azocasein + H2O | excellent substrate for mouse, poorer substrate for rat and human enzymes | Mus musculus | fragments of azocasein | - |
? | |
azocasein + H2O | excellent substrate for mouse, poorer substrate for rat and human enzymes | Homo sapiens | fragments of azocasein | - |
? | |
azocasein + H2O | excellent substrate for mouse, poorer substrate for rat and human enzymes | Rattus norvegicus | fragments of azocasein | - |
? | |
azocasein + H2O | excellent substrate for mouse, poorer substrate for rat and human enzymes | Homo sapiens PPH | fragments of azocasein | - |
? | |
Big endothelin I + H2O | rat | Rattus norvegicus | ? | - |
? | |
bradykinin + H2O | - |
Mus musculus | Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg | - |
? | |
bradykinin + H2O | - |
Homo sapiens | Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg | - |
? | |
bradykinin + H2O | - |
Rattus norvegicus | Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg | - |
? | |
Endothelin I + H2O | rat | Rattus norvegicus | ? | - |
? | |
Gonadotropin + H2O | mouse | Mus musculus | ? | - |
? | |
Human alpha-atrial natiuretic peptide + H2O | rat | Rattus norvegicus | ? | - |
? | |
Human transforming growth factor + H2O | rat | Rattus norvegicus | ? | - |
? | |
Insulin B-chain + H2O | prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 | Mus musculus | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 | Homo sapiens | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 | Rattus norvegicus | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | 10 cleavage sites | Mus musculus | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | 10 cleavage sites | Homo sapiens | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | 10 cleavage sites | Rattus norvegicus | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | 7 major and 3 minor sites | Mus musculus | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | 7 major and 3 minor sites | Homo sapiens | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | 7 major and 3 minor sites | Rattus norvegicus | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | oxidized form | Mus musculus | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | oxidized form | Homo sapiens | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | oxidized form | Rattus norvegicus | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 | Homo sapiens PPH | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | 10 cleavage sites | Homo sapiens PPH | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | 7 major and 3 minor sites | Homo sapiens PPH | Hydrolyzed insulin B-chain | - |
? | |
Insulin B-chain + H2O | oxidized form | Homo sapiens PPH | Hydrolyzed insulin B-chain | - |
? | |
N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O | i.e. PABA-peptide, rat, human, arylamidolysis | Homo sapiens | N-Benzoyl-L-tyrosine + 4-aminobenzoate | - |
? | |
N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O | i.e. PABA-peptide, rat, human, arylamidolysis | Rattus norvegicus | N-Benzoyl-L-tyrosine + 4-aminobenzoate | - |
? | |
neurotensin + H2O | i.e. pyro-Glu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu, mouse, rat, cleavage sites: Glu-Asn, Asn-Lys | Mus musculus | ? | - |
? | |
neurotensin + H2O | i.e. pyro-Glu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu, mouse, rat, cleavage sites: Glu-Asn, Asn-Lys | Rattus norvegicus | ? | - |
? | |
Substance P + H2O | - |
Homo sapiens | Hydrolyzed substance P | - |
? | |
Substance P + H2O | rat | Rattus norvegicus | Hydrolyzed substance P | - |
? | |
[Met5]enkephalin-Arg6-Phe7 + H2O | - |
Mus musculus | ? | - |
? | |
[Met5]enkephalin-Arg6-Phe7 + H2O | - |
Homo sapiens | ? | - |
? | |
[Met5]enkephalin-Arg6-Phe7 + H2O | - |
Rattus norvegicus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the mouse enzyme is composed of disulfide linked dimers associating non-covalently to form tetramers and sometimes higher order oligomers | Mus musculus |
More | the mouse enzyme is composed of disulfide linked dimers associating non-covalently to form tetramers and sometimes higher order oligomers | Rattus norvegicus |
oligomer | x * 90000, mouse, SDS-PAGE, reducing conditions | Mus musculus |
oligomer | x * 90000, mouse, SDS-PAGE, reducing conditions | Rattus norvegicus |
tetramer | 4 * 85000, mouse | Mus musculus |
tetramer | 4 * 85000, mouse | Rattus norvegicus |
tetramer | in the presence of 2-mercaptoethanol | Mus musculus |
tetramer | in the presence of 2-mercaptoethanol | Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Mus musculus |
30 | - |
nitrobradykinin assay | Mus musculus |
37 | - |
assay at | Mus musculus |
37 | - |
assay at | Homo sapiens |
37 | - |
assay at | Rattus norvegicus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.1 | - |
2-Aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
2.4 | - |
2-Aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
4.9 | - |
2-Aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
5 | - |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg | - |
Mus musculus | |
7.6 | - |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg | - |
Mus musculus | |
12 | - |
2-Aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
19.6 | - |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg | - |
Mus musculus | |
26.7 | - |
2-Aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
40.9 | - |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg | - |
Mus musculus | |
51.5 | - |
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg | - |
Mus musculus | |
98.5 | - |
2-Aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus | |
133 | - |
2-Aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg | - |
Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
pI: multiple bonds in the range of 4-5, presumably due to glycosylation | Mus musculus |
additional information | - |
pI: multiple bonds in the range of 4-5, presumably due to glycosylation | Homo sapiens |
additional information | - |
pI: multiple bonds in the range of 4-5, presumably due to glycosylation | Rattus norvegicus |