The binding requirements of monkey brain lysosomal enzymes to their immobilised receptor protein

Keith Alvares*, K. Panneerselvam, A. S. Balasubramanian

*Corresponding author for this work

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

The lysosomal enzyme binding protein (receptor protein) isolated from monkey brain was immobilised on Sepharose 4B and used to study the binding of brain lysosomal enzymes. The immobilised protein could bind \-D-glucosaminidase, α-D-mannosidase, α-L-fucosidase and2-D-glucuronidase. The bound enzymes could be eluted either at an acid pH of 4.5 or by mannose 6-phosphate but not by a number of other sugars tested. Binding could be abolished by prior treatment of the lysosomal enzymes with sodium periodate. Alkaline phosphatase treatment of the enzymes did not prevent the binding of the lysosomal enzymes to the column but decreased their affinity, as seen by a shift in their elution profile, when a gradient elution with mannose 6-phosphate was employed. These results suggested that an 'uncovered' phosphate on the carbohydrate moiety of the enzymes was not essential for binding but can enhance the binding affinity.

Original languageEnglish (US)
Pages (from-to)215-225
Number of pages11
JournalJournal of Biosciences
Volume10
Issue number2
DOIs
StatePublished - Jun 1 1986

Keywords

  • Lysosomal enzyme binding protein
  • binding requirements
  • brain
  • immobilisation

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)

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