Results 221 to 230 of about 80,553 (266)
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Association Of An Integral Membrane Protein With Glucose Transport And With Anion Transport
Journal of Cell Science, 1984ABSTRACT 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, 1982The 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, 1985The 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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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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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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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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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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Denaturation of a membrane transport protein by urea: The erythrocyte anion exchanger
The Journal of Membrane Biology, 1987Chloride equilibrium exchange was measured in the presence of intracellular and extracellular urea, several different alkylureas and thiourea. Urea half-inhibited Cl exchange at about 2.5 M, but the other, less polar analogs had significantly higher potencies; e.g., butylurea half-inhibited at about 60 mM.
O, Fröhlich, S C, Jones
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The Impact of Plasma Protein Binding on the Renal Transport of Organic Anions
The Journal of Pharmacology and Experimental Therapeutics, 2006Drugs and xenobiotics bind to plasma proteins with varying degrees of affinity, and the amount of binding has a direct effect on free drug concentration and subsequent pharmacokinetics. Multiple active and facilitative transport systems regulate the excretion of anionic compounds from the blood in excretory and barrier tissues.
Daniel A J, Bow +3 more
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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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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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Conformation and stability of the anion transport protein of human erythrocyte membranes
Biochemistry, 1985The conformation and stability of purified preparations of band 3, the anion transport protein of human erythrocyte membranes, and its constituent proteolytic subfragments have been studied by circular dichroism. Band 3, purified in the presence of the nonionic detergent n-dodecyl octaethylene glycol monoether (C12E8), had an alpha-helical content of ...
K, Oikawa +2 more
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Archives of Biochemistry and Biophysics, 1990
The effect of streptozotocin-induced diabetes on the levels of functional mitochondrial anion transport proteins has been determined. The experimental approach utilized for these studies consisted of the extraction of each of four mitochondrial anion transport proteins from rat liver mitoplasts (isolated from diabetic and control animals) with the ...
Ronald S Kaplan, Glenn L Wilson
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The effect of streptozotocin-induced diabetes on the levels of functional mitochondrial anion transport proteins has been determined. The experimental approach utilized for these studies consisted of the extraction of each of four mitochondrial anion transport proteins from rat liver mitoplasts (isolated from diabetic and control animals) with the ...
Ronald S Kaplan, Glenn L Wilson
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