Inhibitors | Comment | Organism | Structure |
---|---|---|---|
pepstatin A | - |
Patiria pectinifera |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
50000 | - |
SDS-PAGE | Patiria pectinifera |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Patiria pectinifera | - |
- |
- |
Purification (Comment) | Organism |
---|---|
purified by ammonium sulfate precipitation and octyl sepharose, Con-A sepharose, CM-sephadex columns sequentially. Finally, by preparative gel electrophoresis. On SDS-PAGE the purified preparation gives two bands 50 kDa and 47 kDa. The upper band is characterized as cathepsin D and the lower band as sialidase. The two enzymes are separated from each other by using high-performance gel-filtration chromatography | Patiria pectinifera |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.15 | - |
after preparative PAGE (gel concentration 7%) | Patiria pectinifera |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-Phe-Arg-Leu-Lys(Dnp)-D-Arg-NH2 + H2O | - |
Patiria pectinifera | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
cathepsin D | - |
Patiria pectinifera |