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Ultracentrifugation studies on the transmembrane domain of the human erythrocyte anion transporter band 3 in the detergent C12E8.

Abstract:

The dilute solution behaviour of the transmembrane domain (TMD) of the human erythrocyte anion exchanger Band 3 was studied by analytical ultracentrifugation. Sedimentation velocity and equilibrium studies of the TMD solubilized with the detergent C12E8 demonstrate that the protein is a stable dimer in the concentration range 0.1 to 1 mg/ml. There is no evidence of a dissociation at low concentrations or of an association at higher concentrations. Hydrodynamic calculations applying a prolate ...

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Publication status:
Published

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Publisher copy:
10.1007/s002490050177

Authors


Cölfen, H More by this author
Boulter, JM More by this author
Harding, SE More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
European biophysics journal : EBJ
Volume:
27
Issue:
6
Pages:
651-655
Publication date:
1998
DOI:
EISSN:
1432-1017
ISSN:
0175-7571
URN:
uuid:55ae1df2-d32a-4bd7-91ff-06811712c190
Source identifiers:
410506
Local pid:
pubs:410506

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