Decreased rotational diffusion of band 3 in melanesian ovalocytes from Papua,New Guinea |
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| Authors: | Leann Tilley Gerard B. Nash Graham L. Jones William H. Sawyer |
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| Affiliation: | (1) Department of Biochemistry, La Trobe University, 3083 Bundoora, Victoria, Australia;(2) Department of Haematology, The Medical School, University of Birmingham, Birmingham, United Kingdom;(3) Queensland Institute of Medical Research, 4006 Herston, Queensland, Australia;(4) Department of Biochemistry, University of Melbourne, 3052 Parkville, Victoria, Australia |
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| Abstract: | Summary Melanesian ovalocytes from Papua New Guinea have an N-terminal extension of the band 3 polypeptide (Jones, G.L., Edmunson. H.M., Wesche, D., Saul, A. 1990.Biochim. Biophys. Acta1096:33–40). The ovalocytes showed a threefold increase in shear elastic modulus as determined by micropipette aspiration measurements of membrane rigidity. Time-resolved phosphorescence anisotropy has been used to study the rotational freedom of band 3 in membranes prepared from ovalocytes. The ovalocytic polymorphism was found to be associated with a marked decrease in the rotational mobility of band 3. This may indicate participation of band 3 in large homoaggregates or in complexes with other proteins at the cytoplasmic surface. There was no morphological clustering of band 3 detectable by immunofluorescence microscopy. |
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| Keywords: | band 3 rotational diffusion ovalocytosis erythrocyte membrane membrane rigidity |
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