| Autor: |
Balasubramanian, A., Alam, T., Mathur, R., Lakshmi, S., Cherian, R., Alvares, K. |
| Zdroj: |
Journal of Biosciences; December 1983, Vol. 5 Issue: Supplement 1 p61-64, 4p |
| Abstrakt: |
Abstract: Concanavalin A bound to Sepharose has been used for the purification of brain β-galactosidase, α-L-fucosidase, α-D-mannosidase, arylsulphatase and β-glucuronidase.0 Several factorsviz pH, temperature and concentration of α-methyl glucoside influenced the binding and elution of these enzymes. A lysosomal acid α-mannosidase and a cytosolic neutral mannosidase were separable by concanavalin A-Sepharose chromatography. Similarly lysosomal and microsomal β-glucuronidases were separable using gradient elution with α-methyl glucoside. The results indicate the usefulness of this lectin for the isolation of wide variety of enzymes under specified experimental conditions. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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