Two-step affinity-chromatographic purification of cathepsin D from pig myometrium with high yield
| Autor: | E G Afting, M L Recker |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Swine
Sodium chemistry.chemical_element Cathepsin D Biochemistry Chromatography Affinity Affinity chromatography Pepstatins Concanavalin A Animals Urea Molecular Biology chemistry.chemical_classification Chromatography biology Sepharose Uterus Myometrium Cell Biology Cathepsins Electrophoresis Enzyme chemistry Yield (chemistry) biology.protein Electrophoresis Polyacrylamide Gel Female Research Article |
| Zdroj: | Biochemical Journal. 197:519-522 |
| ISSN: | 0264-6021 |
| Popis: | Cathepsin D was purified by two-step affinity chromatography on concanavalin A- and pepstatin-Sepharose. The main purification was achieved by washing the enzyme bound to the pepstatin-Sepharose column with buffered 6 M-urea. This step separated cathepsin D from all low- and high-molecular-weight impurities. Although the 1700-fold purified acid proteinase was homogeneous on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, it still showed microheterogeneity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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