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

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

*Corresponding author for this work

Research output: Contribution to journalArticle

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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 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 languageEnglish (US)
Pages (from-to)61-64
Number of pages4
JournalJournal of Biosciences
Volume5
Issue number1 Supplement
DOIs
StatePublished - Dec 1 1983

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Keywords

  • Concanavalin A
  • brain hydrolases
  • chromatography

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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