Anion exchange protein

Jay, D., and Candey, L., 1986. Structural a.spects of die red cell anion exchange protein. Annual Review of Biochemistry 55 511-538. 

The major proteins (which include spectrin, ankyrin, the anion exchange protein, actin, and band 4.1) have been studied intensively, and the principal features of their disposition (eg, integral or peripheral), structure, and function have been established. 

The Major Integral Proteins of the Red Blood Cell Membrane Are the Anion Exchange Protein the Glycophorins... 

The anion exchange protein (band 3) is a transmembrane glycoprotein, with its carboxyl terminal end on the external surface of the membrane and its amino terminal end on the cytoplasmic surface. It is an example of a multipass membrane protein, extending across the... 

The number of enzymes and functional proteins that are reportedly regulated by S-nitrosation is on the rise. For example, a search of PUBMED with the key word S-nitrosation revealed some 70 reports of in vitro regulation of enzymes, proteins and cellular processes that are affected by S-nitrosation. Some of these processes that have been well characterized include, nuclear regulatory proteins the NMDA receptor and the ertrocyte anion exchange protein 1 (AE1) (see review by Gaston, 2003). 

Tvo additional peripheral membrane proteins anchor the spectrin filaments to the cytoplasmic side of the erythrocyte membrane. One of these polypeptides, the 210-kDa ankyrin protein, binds both a single spectrin molecule and the chloride-bicarbonate anion-exchange protein discussed previously. The second of these polypeptides, actin, is capable of binding several molecules of spectrin. Since actin is able to associate with more than a single spectrin monomer, it acts as a branch point for the spectrin protein as the membrane skeleton or matrix is assembled (see Fig. 13-1). In this experiment, you will determine the concentration of total protein in the erythrocyte membrane through the use of the Folin-Ciocalteau assay. 

How NO disembarks from the S-nitrosylated Hb and how it is delivered to the neighboring cells has long been not understood. There is now experimental evidence that this process requires a further protein that is present in abundant amounts in the cell membrane of red blood cells, the anion exchanger protein A El (review Pawloski and Stamler, 2002). AE1 appears to be the primary recipient of NO groups from S-nitro-sylated Hb and seems to accept the NO group directy from Hb, a step that is essential for the efflux of NO s biological activity from red blood cells. 

The integral membrane proteins glycophorin and anion exchange protein are components in a network of linkages that connect the plasma membrane to structural elements of the cytoskeleton (e.g., actin, spectrin, protein 4.1, and ankyrin). 

On a weak anion exchanger, proteins are not only applied at high pH but are also retained. The mobile phase contains buffers with a mixture of amino groups with different pJCj and with buffering capacity covering the whole pH range (polybuffers). 

Gerstner JA, Cramer SM. Heparin as a nontoxic displacer for anion-exchange protein displacement systems. BioPharm 1992 11 42-45. 

Liu DS, Kennedy SD and Knauf PA (1996) Source of transport site asymmetry in the band-3 anion exchange protein determined by NMR measurements of external Cr affinity. Biochemistry 35 15228-15235. 

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