The Anion Transport Protein

Structure and Function
  • Michael L. Jennings
Part of the Contemporary Biomedicine book series (CB, volume 10)


The major 95 kdalton transmembrane protein of the red-cell membrane, denoted band 3 (Fairbanks et al., 1971) or capnophorin (Wieth and Bjerrum, 1983), catalyzes a tightly coupled exchange of anions. The purpose of this chapter is to summarize the current state of knowledge regarding the structure of this protein, with emphasis on those aspects of the structure that relate to anion transport. The amount of information currently available about band 3 is quite large, and this chapter will deal only superficially with several important topics that are somewhat related to the transport mechanism. These include lateral and rotational mobility of the protein (Beth et al., 1986; Mühlebach and Cherry, 1985); carbohydrate composition and structure (Tsuji et al., 1981; Fukuda et al., 1984); band 3 biosynthesis (Braell and Lodish, 1981); role of band 3 in red-cell senescence (Kay, 1984; Low et al., 1985); interaction with lipids (Köhne et al., 1983); and the physiology of CO2 exchange in the pulmonary and systemic capillaries (see Wieth et al., 1982). Certain other topics that relate centrally to the transport mechanism, including transport kinetics, reversible inhibitors, pH dependence, and chemical modification of arginine residues and carboxyl groups, are discussed in detail in Chapters 9 and 15.


Lysine Residue Cytoplasmic Domain Human Erythrocyte Membrane Domain Anion Transport 
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© The Humana Press Inc. 1989

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  • Michael L. Jennings

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