1980•PubMedRequires access

Morphological characterization of the erythrocyte membrane related to myxovirus receptors.

I Bächi

Open publisher page 1 citations

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.

About this research paper

What this paper is about

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.

Why it matters

OpenAlex reports 1 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available 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.

Key concepts: Glycophorin, Sialoglycoprotein, Sialic acid, Sialoglycoproteins, Lectin, Glycoprotein, Biochemistry, Membrane

Related papers

Back to paper searchBrowse research topicsOriginal source
Morphological characterization of the erythrocyte membrane related to myxovirus receptors. — Research Paper | ScholarLens