Biochemical characterization of cathepsin D from the mussel Lamellidens corrianus
Biochemical characterization of cathepsin D from the mussel Lamellidens corrianus
| dc.contributor.author | Venugopal, Ashapogu | |
| dc.contributor.author | Siva Kumar, Nadimpalli | |
| dc.date.accessioned | 2022-03-27T04:51:40Z | |
| dc.date.available | 2022-03-27T04:51:40Z | |
| dc.date.issued | 2014-01-01 | |
| dc.description.abstract | A lysosomal cathepsin D (EC 3.4.23.5) was purified to homogeneity from the soft tissues of the fresh water mussel (Lamellidens corrianus) by pepstatin A affinity chromatography. The purified enzyme is a glycoprotein and migrates as a single protein species in native PAGE and shows a single band in SDS-PAGE corresponding to a molecular mass of ~43kDa. Under both these conditions cathepsin D hydrolyzes hemoglobin as shown by zymogram analysis. The purified enzyme cross-reacts with an antiserum to purified starfish (Asterias rubens) cathepsin D. Additionally, the enzyme was recognized by the starfish lysosomal enzyme targeting receptors (mannose 6-phosphate receptors: MPR 300 and 46) in ligand blot analysis. The KM value of the purified enzyme with hemoglobin is 1.5mM. pH and temperature optimum for the enzyme are 3.5 and 60°C respectively. © 2013 Elsevier Inc. | |
| dc.identifier.citation | Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology. v.169(1) | |
| dc.identifier.issn | 10964959 | |
| dc.identifier.uri | 10.1016/j.cbpb.2013.12.003 | |
| dc.identifier.uri | https://www.sciencedirect.com/science/article/abs/pii/S1096495913002108 | |
| dc.identifier.uri | https://dspace.uohyd.ac.in/handle/1/7222 | |
| dc.subject | Cathepsin D | |
| dc.subject | Invertebrate | |
| dc.subject | Lamellidens corrianus | |
| dc.subject | Mannose 6-phosphate receptor | |
| dc.subject | Zymogram | |
| dc.title | Biochemical characterization of cathepsin D from the mussel Lamellidens corrianus | |
| dc.type | Journal. Article | |
| dspace.entity.type |
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