Morphological characterization of the erythrocyte membrane related to myxovirus receptors.
I Bächi
Abstract
I Bächi
Abstract
The receptor of myxoviral hemagglutinins is defined by terminal sialic acid residues of the major sialoglycoprotein (glycophorin) of the human erythrocyte membrane. A number of lectins and antibodies are suitable to specifically label this molecule. The proposed association of glycophorin with the structures revealed as intramembrane particles (IMP) on freeze-fractured membranes rests only on indirect evidence; IMP are not composed of glycophorin alone but glycophorin may be a component of them in association with other integral membrane proteins and/or lipids. Mapping experiments employing limulin, a lectin specific for sialic acids, and anti-glycophorin are described. These experiments demonstrate a lack of association of glycophorin and the IMP.
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The receptor of myxoviral hemagglutinins is defined by terminal sialic acid residues of the major sialoglycoprotein (glycophorin) of the human erythrocyte membrane. A number of lectins and antibodies are suitable to specifically label this molecule. The proposed association of glycophorin with the structures revealed as intramembrane particles (IMP) on freeze-fractured membranes rests only on indirect evidence; IMP are not composed of glycophorin alone but glycophorin may be a component of them in association with other integral membrane proteins and/or lipids. Mapping experiments employing limulin, a lectin specific for sialic acids, and anti-glycophorin are described. These experiments demonstrate a lack of association of glycophorin and the IMP.
Key concepts: Glycophorin, Sialoglycoprotein, Sialic acid, Sialoglycoproteins, Lectin, Glycoprotein, Biochemistry, Membrane