Results 341 to 350 of about 373,177 (393)

Macromolecular conjugates of transport inhibitors: new tools for probing topography of anion transport proteins

American Journal of Physiology-Cell Physiology, 1991
Macromolecular-conjugated, water-soluble, membrane-impermeant compounds were designed and assessed as topological probes for chloride-transporting agencies. The novel compounds were derivatives of either disulfonic stilbene (DS) and benzylaminoethylsulfonate (BS), "classical" inhibitors of erythrocyte chloride-bicarbonate exchange, or of ...
R. Greger, H. G. Lang, H. C. Englert, Z. I. Cabantchik, O. Eidelman, P. Yani   +5 more
openaire   +3 more sources

Transepithelial Transport of Organic Anions across the Choroid Plexus: Possible Involvement of Organic Anion Transporter and Multidrug Resistance-Associated Protein

The Journal of Pharmacology and Experimental Therapeutics, 1999
Transport characteristics of 17beta-estradiol 17beta-D-glucuronide (E217betaG), a dual substrate of the transporters for cellular uptake (organic anion-transporting polypeptide 1 or oatp1) and cellular excretion (multidrug resistance-associated protein 1or MRP1), in the rat choroid plexus were studied in vivo and in vitro.
J, Nishino, H, Suzuki, D, Sugiyama, T, Kitazawa, K, Ito, M, Hanano, Y, Sugiyama   +6 more
openaire   +2 more sources

Dichotomous development of the organic anion transport protein in liver and choroid plexus

American Journal of Physiology-Cell Physiology, 1998
Both adult liver and choroid plexus express the organic anion transport protein (oatp1) and transport [35S]bromosulfophthalein (BSP). Studies of the developing rat liver reveal that oatp1 mRNA and protein do not begin to be expressed until 15 days postnatal and are at adult levels by 30 days. Uptake of [35S]BSP follows the same time course.
Phyllis M. Novikoff, Ari J. Bergwerk, Ruth Hogue Angeletti, Allan W. Wolkoff   +3 more
openaire   +3 more sources

Immunologic distribution of an organic anion transport protein in rat liver and kidney

American Journal of Physiology-Gastrointestinal and Liver Physiology, 1996
A Na(+)-independent organic anion transport protein was recently cloned from rat liver using a Xenopus laevis oocyte expression system [E. Jacquemin, B. Hagenbuch, B. Stieger, A.W. Wolkoff, and P.J. Meier, Proc. Natl. Acad. Sci. USA 91: 133-137, 1994].
Bergwerk, A. J., Shi, X., Ford, A. C., Kanai, N., Jacquemin, E., Burk, R. D., Bai, S., Novikoff, P. M., Stieger, B., Meier, P. J., Schuster, V. L., Wolkoff, A. W.   +11 more
openaire   +3 more sources

Oxyanion selectivity in sulfate and molybdate transport proteins: an ab initio/CDM study.

Journal of the American Chemical Society, 2004
A striking feature of sulfate (SO(4)(2-)) and molybdate (MoO(4)(2-)) transport proteins, such as SBP and ModA, which specifically bind SO(4)(2-) and MoO(4)(2-), respectively, is their ability to discriminate very similar anions with the same net charge ...
T. Dudev, C. Lim
semanticscholar   +1 more source

A role for band 4.2 in human erythrocyte band 3 mediated anion transport.

Biochemistry, 1993
Human erythrocyte band 3 was purified essentially free of peripheral proteins, in particular band 4.2, using affinity chromatography. Band 3 protein was then reconstituted into liposomes of lipid type and ratio approximating that of erythrocyte membranes.
S. Malik, M. Sami, A. Watts
semanticscholar   +1 more source

STRUCTURE OF THE ERYTHROCYTE ANION TRANSPORT PROTEIN [PDF]

Biochemical Society Transactions, 1981
C. J. Brock, Michael J. A. Tanner
openaire   +1 more source

Molecular characterization of the human erythrocyte anion transport protein in octyl glucoside

Biochemistry, 1985
Band 3 protein, the anion transport protein of the human erythrocyte membrane, was purified in the presence of the nonionic detergent octyl glucoside. A molecular characterization was carried out to investigate whether the native structure of the protein was retained in the presence of this detergent.
Pamela K. Werner, Reinhart A. F. Reithmeier   +1 more
openaire   +3 more sources

The red cell band 3 protein: its role in anion transport

Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1982
Studies of anion transport across the red blood cell membrane fall generally into two categories: (1) those concerned with the operational characterization of the transport system, largely by kinetic analysis and inhibitor studies; and (2) those concerned with the structure of band 3, a transmembrane peptide identified as the transport protein.
M Ramjeesingh, A Rothstein
openaire   +3 more sources

Isoforms of SLC26A6 mediate anion transport and have functional PDZ interaction domains.

American Journal of Physiology - Cell Physiology, 2003
The solute carrier gene family SLC26 consists of tissue-specific anion exchanger genes, three of them associated with distinct human recessive disorders.
H. Lohi, G. Lamprecht, D. Markovich, Anders Heil, M. Kujala, U. Seidler, J. Kere   +6 more
semanticscholar   +1 more source