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Expression of Anion Exchanger 1 (AE1) and Its Potential Involvement in Human Granulosa Cell Physiology: An In Vitro Pilot Study. [PDF]

Biomolecules
Marin L, Sabbadin C, Radu CM, Brun P, Frison C, Gullo G, Armanini D, Bordin L, Ragazzi E, Ambrosini G, Andrisani A.   +10 more
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Structure and Function of Mitochondrial Anion Transport Proteins

Journal of Membrane Biology, 2001
R S Kaplan
exaly   +3 more sources

Transport domain of the erythrocyte anion exchange protein

The Journal of Membrane Biology, 1990
The anion transport domain of the anion exchange protein (AEP) of human erythrocyte membranes (band 3, 95 kD mol wt) was probed with the substrate and affinity label pyridoxal-5'-phosphate (PLP). Acting from outside, this probe labels two chymotryptic fragments of 65 and 35 kD of AEP but only the 35-kD fragment is protected from labeling by reversibly ...
S, Bar-Noy, Z I, Cabantchik
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Catabolism of the anion transport protein in human erythrocytes

Biochemistry, 1985
We identified the catabolic products of protein 3 in human erythrocytes. Protein 3, the major protein of the erythrocyte membrane, functions in anion transport and reacts covalently with tritiated 4,4'-diisothiocyano-1,2-diphenylethane-2,2'-disulfonic acid ([3H]DIDS), a very selective inhibitor of anion transport.
M, Morrison, W, Grant, H T, Smith, T J, Mueller, L, Hsu   +4 more
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Association Of An Integral Membrane Protein With Glucose Transport And With Anion Transport

Journal of Cell Science, 1984
ABSTRACT A monoclonal antibody that recognizes a cell-surface glycoprotein associated with glucose transport was reported previously. Additional information about the function and intracellular distribution of the antigen recognized by this antibody is presented.
M R, Banyard, M K, White
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The erythrocyte anion transport protein is cotranslationally inserted into microsomes

Cell, 1982
The biosynthesis of the erythrocyte anion transport protein, Band III (molecular weight 100,000), is of interest, as its NH2-terminal half is hydrophilic and faces the cytoplasmic surface, and its COOH-terminal half spans the phospholipid bilayer several times.
W A, Braell, H F, Lodish
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A new variant of the anion transport protein in human erythrocytes

Biochemistry, 1985
The major plasma membrane protein of human erythrocytes is the anion transport protein, termed protein 3. We previously reported a variant form of protein 3 that is elongated on the amino-terminal end of the molecule, which is exposed on the cytoplasmic side of the membrane, but otherwise its features are identical with those of the normal molecule. We
L, Hsu, M, Morrison
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The Anion Transport Protein

1989
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 ...
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Regulation by protein kinase C of organic anion transport driven by rat organic anion transporter 3 (rOAT3)

Life Sciences, 2000
The organic anion transporter 3 (rOAT3) is a multispecific OAT localized at the basolateral membrane of the proximal tubule. The purpose of this study was to elucidate the role of protein kinase C (PKC) in the regulation of organic anion transport driven by rOAT3 and its mechanism of action.
M, Takeda, T, Sekine, H, Endou
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Characterization of the anion transport channel protein in human erythrocytes. Induced circular dichroism of inhibitors bound to the anion transport channel

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1986
The induced circular dichroism (CD) of erythrocyte ghosts with anion-transport inhibitors has been studied. A ghost-EITC (eosin 5-isothiocyanate) system shows an induced CD spectrum at the wavelength region corresponding to the absorption bands of EITC.
Y, Sato, T, Chiba, Y, Suzuki
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