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. 1988 Jan;85(2):492–496. doi: 10.1073/pnas.85.2.492

Functional topography of band 3: specific structural alteration linked to functional aberrations in human erythrocytes.

M M Kay 1, G J Bosman 1, C Lawrence 1
PMCID: PMC279576  PMID: 2829189

Abstract

Band 3 is the major anion transport polypeptide of erythrocytes. It appears to be the binding site of several glycolytic enzymes. Structurally, band 3 is the major protein spanning the erythrocyte membrane and connects the plasma membrane to band 2.1, which binds to the cytoskeleton. In the present study, we report an alteration of band 3 molecule that is associated with the following changes: erythrocyte shape change from discoid to "thorny cells" (acanthocytes), restriction of rotational diffusion of band 3 in the membrane, increase in anion transport, and decrease in the number of high-affinity ankyrin-binding sites. Changes in erythrocyte IgG binding, glyceraldehyde-3-phosphate dehydrogenase, fluorescence polarization (indicative of membrane fluidity), and other membrane proteins as determined by polyacrylamide gel electrophoresis were not detected. Cells containing the altered band 3 polypeptide were obtained from individuals with abnormal erythrocyte morphology. Two-dimensional peptide maps revealed differences in the Mr 17,000 anion transport segment of band 3 consistent with additions of tyrosines or tyrosine-containing peptides. The data suggest that (i) this alteration of band 3 does not result in accelerated aging as does cleavage and (ii) structural changes in the anion transport region result in alterations in anion transport.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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