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Journal Article

The relationships between oligomeric structure and function of band 3 protein from human erythrocyte membranes: present knowledge and suggestions for further experiments

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Schubert,  Dieter
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Schubert, D. (1988). The relationships between oligomeric structure and function of band 3 protein from human erythrocyte membranes: present knowledge and suggestions for further experiments. Molecular Aspects of Medicine, 10(3), 233-237. doi:10.1016/0098-2997(88)90009-x.


Cite as: https://hdl.handle.net/21.11116/0000-0008-4AB0-E
Abstract
Band 3, the main intrinsic protein of the human erythrocyte membrane, is an exceptional membrane protein both structurally and functionally: it is present in the erythrocyte membrane in different oligomeric states, and it has several different biological functions. It thus represents a highly interesting model for studying the relationships between oligomeric structure and function of a membrane protein. However, despite the efforts of many laboratories, information about these relationships is scarce. This paper will give a brief description of the present status of the field. Its main intention is, however, to suggest experiments by which the major open questions could be answered. It is anticipated that the methods suggested will be applicable to the study of the structure-function relationships of a variety of other oligomeric membrane proteins.