Results 321 to 330 of about 373,177 (393)

Structure and Function of Mitochondrial Anion Transport Proteins

Journal of Membrane Biology, 2001
R. S. Kaplan
openaire   +4 more sources

Temporal expression profiles of organic anion transport proteins in placenta and fetal liver of the rat.

American Journal of Physiology. Regulatory Integrative and Comparative Physiology, 2004
Physiological cholestasis linked to immature hepatobiliary transport systems for organic anions occurs in rat and human neonates. In utero, the placenta facilitates vectorial transfer of certain fetal-derived solutes to the maternal circulation for ...
Marie V. St-Pierre, T. Stallmach, A. F. Grundschober, Jean-François Dufour, Maria A. Serrano, Jose J.G. Marin, Y. Sugiyama, Peter J. Meier   +7 more
semanticscholar   +1 more source

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 ...
Z. I. Cabantchik, Shoshana Bar-Noy
openaire   +3 more sources

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.
Li Hsu, Martin Morrison, Harry T. Smith, Thomas J. Mueller, Wilson D. Grant   +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.
Harvey F. Lodish, William A. Braell
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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
Li Hsu, Martin Morrison
openaire   +3 more sources

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.
Hitoshi Endou, Takashi Sekine, Michio Takeda   +2 more
openaire   +3 more sources

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.
Yasuo Suzuki, Yukio Sato, Tadahiko Chiba
openaire   +3 more sources

Asymmetry of functional sites of the erythrocyte anion transport protein

Trends in Biochemical Sciences, 1978
The accessibility of functional sites of the anion transport system of the red blood cell to inhibitory probes differs depending on the side of the membrane to which they are applied. These effects are discussed in terms of the asymmetric arrangement of the transport protein, Band 3, in the membrane.
P A Knauf, A. Rothstein, S. Ship, S. Grinstein   +3 more
openaire   +2 more sources