title: Consequences of the presence of elongated variant of the major transmembrane protein (Band 3 protein) in the human erythrocyte.
abstract: Among 56 persons studied, 6 were heterozygous with respect to the elongated variant of the Band 3 protein (anion transporting protein) of the erythrocyte membranes. Erythrocytes containing the variant Band 3 protein did not exhibit morphologic abnormalities, alterations in electron spin resonance spectra of maleimide-spin labeled membranes. In the rate of membrane 'self-digestion' or in chloride permeability. They did however show an increased membrane binding of hemoglobin and aldolase.
authors.affiliation: Department of Biophysics, University of Lódź, Poland.
authors.forename: W
authors.initials: W
authors.lastname: Retelewska
authors.forename: M
authors.initials: M
authors.lastname: Gaczyńska
authors.forename: G
authors.initials: G
authors.lastname: Bartosz
authors.forename: L
authors.initials: L
authors.lastname: Judkiewicz
mesh_terms: D001457:Anion Exchange Protein 1, Erythrocyte / Q000032:analysis* / Q000235:genetics; D002712:Chlorides / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000737:chemistry* / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D006579:Heterozygote; D006801:Humans
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D002712:Chlorides; D006454:Hemoglobins; D005634:Fructose-Bisphosphate Aldolase