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.

Membrane anchoring and surface distribution of glycohydrolases of human erythrocyte membrane / G. Goi, C. Bairati, L. Massaccesi, A. Lovagnini, A. Lombardo, G. Tettamanti. - In: FEBS LETTERS. - ISSN 0014-5793. - 473:1(2000), pp. 89-94.

Membrane anchoring and surface distribution of glycohydrolases of human erythrocyte membrane

G. Goi
Primo
;
C. Bairati
Secondo
;
L. Massaccesi;A. Lombardo
Penultimo
;
G. Tettamanti
Ultimo
2000

Abstract

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.
Erythrocyte ghost; Glycan phosphoinositide anchor; Glycohydrolase; Human erythrocyte; Membrane microdomain
Settore BIO/12 - Biochimica Clinica e Biologia Molecolare Clinica
Settore MED/46 - Scienze Tecniche di Medicina di Laboratorio
2000
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/166444
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