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The use of concanavalin A in the purification or separation of multiple forms of brain hydrolases

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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.

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Authors and Affiliations

  1. Neurochemistry Laboratory, Department of Neurological Sciences, Christian Medical College Hospital, 632 004, Vellore

    A. S. Balasubramanian, T. Alam, R. Mathur, S. Lakshmi, R. Cherian & K. Alvares

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  1. A. S. Balasubramanian
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  2. T. Alam
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  3. R. Mathur
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  4. S. Lakshmi
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  5. R. Cherian
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  6. K. Alvares
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Balasubramanian, A.S., Alam, T., Mathur, R. et al. The use of concanavalin A in the purification or separation of multiple forms of brain hydrolases. J Biosci 5 (Suppl 1), 61–64 (1983). https://doi.org/10.1007/BF02702975

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  • DOI: https://doi.org/10.1007/BF02702975

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