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 factors viz 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.
Original language | English (US) |
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Pages (from-to) | 61-64 |
Number of pages | 4 |
Journal | Journal of Biosciences |
Volume | 5 |
Issue number | 1 Supplement |
DOIs | |
State | Published - Dec 1 1983 |
Keywords
- Concanavalin A
- brain hydrolases
- chromatography
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Agricultural and Biological Sciences(all)