Membrane anchoring and surface distribution of glycohydrolases of human erythrocyte membranes

Giancarlo Goi, Chiara Bairati, Luca Massaccesi, Augusto Lovagnini, Adriana Lombardo, Guido Tettamanti

Research output: Contribution to journalArticlepeer-review


The membrane anchoring of the following glycohydrolases of human erythrocyte plasma membranes was investigated: α- and β-D-glucosidase, α- and β-D-galactosidase, β-D-glucuronidase, N-acetyl-β-D-glucosaminidase, α-D-mannosidase, and α-L-fucosidase. Optimized fluorimetric methods for the assay of these enzymes were set up. Treatment of the ghost preparation with 1.0 mol/l (optimal concentration) NaCl caused release ranging from 4.2% of α-D-glucosidase to 70% of β-D-galactosidase; treatment with 0.4% (optimal concentration) Triton X-100 liberated 5.1% of β-D-galactosidase to 89% of α-D-glucosidase; treatment with 1.75% (optimal concentration) octylglucoside yielded solubilization from 6.3% of β-D-galactosidase to 85% of α-D-glucosidase. Treatment with phosphoinositide-specific phospholipase C caused no liberation of any of the studied glycohydrolases. These results are consistent with the notion that the above glycohydrolases are differently anchored or associated with the erythrocyte plasma membrane, and provide the methodological basis for inspecting the occurrence of these enzymes in different membrane microdomains. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)89-94
Number of pages6
JournalFEBS Letters
Issue number1
Publication statusPublished - May 4 2000


  • Erythrocyte ghost
  • Glycan phosphoinositide anchor
  • Glycohydrolase
  • Human erythrocyte
  • Membrane microdomain

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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