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Literature summary for 3.4.23.5 extracted from

  • Takahashi, T.; Tang, J.
    Cathepsin D from porcine and bovine spleen (1981), Methods Enzymol., 80, 564-581.
No PubMed abstract available

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
12000
-
1 * 12000 + 1 * 34000, the enzyme also exists as a single chain enzyme form Bos taurus
15000
-
1 * 15000 + 1 * 35000, isoenzyme I, II, III and IV, SDS-PAGE Sus scrofa
34000
-
1 * 12000 + 1 * 34000, the enzyme also exists as a single chain enzyme form Bos taurus
35000
-
1 * 15000 + 1 * 35000, isoenzyme I, II, III and IV, SDS-PAGE Sus scrofa
46000
-
1 * 46000, the enzyme also exists as a two-chain form Bos taurus
50000
-
isoenzymes I, II, III, IV, and V, gel filtration Sus scrofa

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Sus scrofa
-
pig
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification
-
Bos taurus
side-chain modification each isoenzyme contains 8 mannose and 4 glucosamine residues per mol Sus scrofa

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa
isoenzyme A and B Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
spleen
-
Sus scrofa
-
spleen
-
Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Sus scrofa
additional information
-
-
Bos taurus

Subunits

Subunits Comment Organism
dimer 1 * 15000 + 1 * 35000, isoenzyme I, II, III and IV, SDS-PAGE Sus scrofa
dimer 1 * 12000 + 1 * 34000, the enzyme also exists as a single chain enzyme form Bos taurus
monomer isoenzyme V, gel filtration Sus scrofa
monomer 1 * 46000, the enzyme also exists as a two-chain form Bos taurus