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

Balasubramanian, A. S. ; Alam, T. ; Mathur, R. ; Lakshmi, S. ; Cherian, R. ; Alvares, K. (1983) The use of concanavalin A in the purification or separation of multiple forms of brain hydrolases Journal of Biosciences, 5 (Suppl_). pp. 61-64. ISSN 0250-5991

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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 α- glucuronidase. 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 ASepharose 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.

Item Type:Article
Source:Copyright of this article belongs to Indian Academy of Sciences.
Keywords:Concanavalin A; Chromatography; Brain Hydrolases
ID Code:91619
Deposited On:22 May 2012 12:15
Last Modified:19 May 2016 05:21

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