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J. Biol. Chem., Vol. 266, Issue 24, 15726-15737, Aug, 1991
JR Casey and RA Reithmeier
The oligomeric state of human Band 3 (Mr = 95,000), the erythrocyte
membrane anion exchanger, was examined by size exclusion high performance
liquid chromatography in solutions containing the nonionic detergent C12E8
(octaethylene glycol n-dodecyl monoether). Band 3 was heterogeneous with
respect to oligomeric composition, the predominant (70%) species being a
dimer that bound 0.57 mg of C12E8/mg of protein (Stokes radius = 78 A,
s20,w = 6.9 S). Variable amounts of larger oligomers were also present;
however, no evidence for equilibration between oligomeric species was
observed in detergent solution. Analytical and large zone size exclusion
chromatography showed that Band 3 could not be dissociated to monomers,
other than by protein denaturation. The membrane domain of Band 3 (Mr =
52,000) was also dimeric, but without evidence for higher oligomeric forms,
which implies that the interactions responsible for higher associations
involve the cytoplasmic domain. Prelabeling of Band 3 with the anion
exchange inhibitor 4,4'-diisothiocyanostilbene-2,2'-disulfonate had no
effect upon the oligomeric state of either intact Band 3 or its 52-kDa
membrane domain. Band 3 oligomeric state could be reversibly changed in the
membrane by altering the pH of the solution. The fraction of Band 3 not
associated with the cytoskeleton was almost entirely dimeric. Band 3
purified from erythrocytes separated by density gradient centrifugation
revealed that older red cells contained a larger proportion of higher
oligomers than did younger cells. We conclude that Band 3, in the membrane
and in C12E8 solution, exists as a mixture of dimers and larger oligomers.
The higher oligomers interact with the cytoskeleton, increase in amount
with cell age, and are held together by interactions of the cytoplasmic
domain.
Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity
Department of Medicine, University of Toronto, Ontario, Canada.
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