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Literature summary for 3.4.23.34 extracted from

  • Yamamoto, K.; Ueno, E.; Uemura, H.; Kato, Y.
    Biochemical and immunochemical similarity between erythrocyte membrane aspartic proteinase and cathepsin E (1987), Biochem. Biophys. Res. Commun., 148, 267-272.
    View publication on PubMed
Search for more literature for 3.4.23.34

Inhibitors

Inhibitors Comment Organism Structure
pepstatin
-
 Homo sapiens
pepstatin
-
 Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane in latent form Homo sapiens 16020
-
membrane in latent form Rattus norvegicus 16020
-
membrane on cytoplasmic face of the membrane Homo sapiens 16020
-
membrane on cytoplasmic face of the membrane Rattus norvegicus 16020
-
soluble active form Homo sapiens
-
-
soluble active form Rattus norvegicus
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41000
-
 2 * 41000, SDS-PAGE, reducing conditions Homo sapiens
41000
-
 2 * 41000, SDS-PAGE, reducing conditions Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Homo sapiens
-
erythrocyte
-
 Rattus norvegicus
-
spleen
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Hemoglobin + H2O acid denatured form Homo sapiens Hydrolyzed hemoglobin
-
 ?
Hemoglobin + H2O acid denatured form Rattus norvegicus Hydrolyzed hemoglobin
-
 ?
Hemoglobin + H2O bovine Homo sapiens Hydrolyzed hemoglobin
-
 ?
Hemoglobin + H2O bovine Rattus norvegicus Hydrolyzed hemoglobin
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 41000, SDS-PAGE, reducing conditions Homo sapiens
dimer 2 * 41000, SDS-PAGE, reducing conditions Rattus norvegicus