Results 271 to 280 of about 164,824 (310)

Protein and buffer transport through anionically grafted nylon membranes

Journal of Membrane Science, 2001
Abstract Microporous nylon 6,6 membranes were modified by grafting poly(2-acrylamido-2-methyl propane sulfonic acid (poly(AMPSA)) on the membrane surface. The poly(AMPSA) grafting on the membrane surface was confirmed by spectroscopic characterization.
S.G Gholap, D.A Musale, S.S Kulkarni, S.K Karode, U.K Kharul   +4 more
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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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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 ...
O, Eidelman, P, Yani, H C, Englert, H G, Lang, R, Greger, Z I, Cabantchik   +5 more
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Computational Analysis of Organic Anion Transport Proteins

2020
This project will use ancestral sequence reconstruction and computational modeling to inform the design of novel function in human OATP proteins with the dual goal of enhanced uptake of MRI contrast agents and non-immunogenic properties. These new functions will allow cells introduced into the body, such as stem cells or immunotherapies to be ...
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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 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.
A, Rothstein, M, Ramjeesingh
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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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Anion transport in relation to proteolytic dissection of band 3 protein

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1978
Sulfate efflux was measured in inside-out vesicles obtained from human red cells. Inhibition was observed in vesicles derived from cells pretreated with DIDS (4,4'-diisothiocyano-2,2'-stilbene disulfonate) or after addition of dipyridamole to the vesicles, both agents being specific and potent inhibitors of anion transport in cells.
S, Grinstein, S, Ship, A, Rothstein
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Structure and Function of the Red Blood Cell Anion Transport Protein

Annual Review of Biophysics and Biophysical Chemistry, 1989
PHYSIOLOGICAL FUNCTION . Role of Chloride-Bicarbonate Exchange in Carbon Dioxide Transport .. Other Substrates of Red Cell Band 3 . . Transport Functions Other Than Anion Exchange . . Band 3 Homologs in Nonerythroid Cells ..
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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.
A. Rothstein, S. Grinstein, S. Ship, P.A. Knauf   +3 more
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