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  • Title: Structural organisation of band 3 in Melanesian ovalocytes.
    Author: Tilley L, McPherson RA, Jones GL, Sawyer WH.
    Journal: Biochim Biophys Acta; 1993 Mar 24; 1181(1):83-9. PubMed ID: 8457610.
    Abstract:
    The diffusional freedom of human erythrocyte band 3 (anion exchanger 1) has been measured in membranes from normocytic and ovalocytic erythrocytes. A dramatic reorganisation of band 3 in the ovalocyte membranes is indicated by a markedly restricted rotational mobility. Extraction of spectrin from erythrocyte membranes had no effect on normocyte band 3 mobility, but partially relieved the restrictions on ovalocyte band 3 mobility. Further removal of ankyrin and band 4.2 resulted in an increase in the rotational mobility of both ovalocyte and normocyte band 3 to similar levels. The results suggest that the molecular basis of the unusual shape and decreased deformability of ovalocytes resides in an altered interaction of band 3 with one or more of the peripheral proteins. We present a model which illustrates a possible role for band 3 aggregation in controlling erythrocyte deformability.
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