Decreased rotational diffusion of band 3 in Melanesian ovalocytes from Papua, New Guinea.
Melanesian ovalcytes 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. Acta 1096:33-40). 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.
Tilley
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Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia.
Nash
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Jones
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Sawyer
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D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004612:Elliptocytosis, Hereditary / Q000097:blood*; D004801:Eosine Yellowish-(YS) / Q000378:metabolism / Q000031:analogs & derivatives; D004907:Erythrocyte Deformability; D004910:Erythrocyte Membrane / Q000737:chemistry*; D004913:Erythrocytes, Abnormal; D005454:Fluorescence Polarization; D006801:Humans; D008288:Malaria / Q000097:blood; D008560:Membrane Fluidity; D008856:Microscopy, Fluorescence; D010219:Papua New Guinea
D001457:Anion Exchange Protein 1, Erythrocyte; C033531:eosin maleimide; D004801:Eosine Yellowish-(YS)