نتایج جستجو برای: anion exchange membrane

تعداد نتایج: 589151  

Journal: :Protein expression and purification 2011
Natsuko Tokuda Kiyohiko Igarashi Tatsuro Shimamura Takami Yurugi-Kobayashi Mitsunori Shiroishi Keisuke Ito Taishi Sugawara Hidetsugu Asada Takeshi Murata Norimichi Nomura So Iwata Takuya Kobayashi

Anion exchangers are membrane proteins that have been identified in a wide variety of species, where they transport Cl(-) and HCO3(-)across the cell membrane. In this study, we cloned an anion-exchange protein from the genome of the basidiomycete Phanerochaete chrysosporium (PcAEP). PcAEP is a 618-amino acid protein that is homologous to the human anion exchanger (AE1) with 22.9% identity and 4...

Journal: :The Journal of General Physiology 1990
M L Jennings R K Schulz M Allen

Tracer anion exchange flux measurements have been carried out in human red blood cells with the membrane potential clamped at various values with gramicidin. The goal of the study was to determine the effect of membrane potential on the anion translocation and binding events in the catalytic cycle for exchange. The conditions were arranged such that most of the transporters were recruited into ...

Journal: :Langmuir : the ACS journal of surfaces and colloids 2013
Zdenek Slouka Satyajyoti Senapati Yu Yan Hsueh-Chia Chang

The physisorption of negatively charged single-stranded DNA (ssDNA) of different lengths onto the surface of anion-exchange membranes is sensitively shown to alter the anion flux through the membrane. At low surface concentrations, the physisorbed DNAs act to suppress an electroconvection vortex instability that drives the anion flux into the membrane and hence reduce the overlimiting current t...

Journal: :Journal of General Physiology 1986

Journal: :The Journal of the Society of Chemical Industry, Japan 1957

Journal: :The Journal of General Physiology 1997
M.N. Chernova L. Jiang M. Crest M. Hand D.H. Vandorpe K. Strange S.L. Alper

Functional evaluation of chemically modified human erythrocytes has led to the proposal that amino acid residue E681 of the band 3 anion exchanger AE1 lies on the anion translocation pathway and is a proton carrier required for H+/SO4(2-) cotransport. We have tested in Xenopus oocytes the functional consequences of mutations in the corresponding residue E699 of mouse AE1. Most mutations tested ...

Journal: :Blood 1990
C H Joiner

Deoxygenation-induced cation movements in sickle cells were inhibited 80% to 85% by the anion transport inhibitor, 4,4'-diisothiocyano-2,2'disulfostilbene (DIDS). Morphologic sickling was not altered by DIDS treatment, demonstrating that morphologic sickling was not sufficient to produce cation leaks in sickle cells. DIDS inhibition of deoxygenation-induced cation flux was not affected when l- ...

Journal: :Eurasian Chemico-Technological Journal 2023

Currently, the main limitation of Anion Exchange Membrane Fuel Cells is related to their low chemical stability under alkaline conditions due degradation quaternary ammonium-based head groups, which lowers transportation hydroxide ions as well. The knowledge intermolecular interaction various ammonium groups with key improving ion’s diffusivity and groups. Consequently, different anion exchange...

Journal: :American journal of physiology. Gastrointestinal and liver physiology 1999
Vazhaikkurichi M Rajendran John Geibel Henry J Binder

A novel Na/H exchange activity that requires Cl was recently identified in the apical membrane of crypt cells of the rat distal colon. This study explores the nature of the coupling of Cl and Na/H exchange. A concentration of 100 μM 5-nitro-2-(3-phenylpropylamino)benzoic acid, a Cl channel blocker, inhibited the Cl dependence of both proton gradient-driven22Na uptake from crypt cell apical memb...

Journal: :Cell 1996
Israel Sekler Sumire Kobayashi Ron R Kopito

Intracellular pH is maintained by a dynamic equilibrium balancing the opposing forces of proton loading and proton extrusion. By providing an efflux pathway for base, anion exchangers constitute a key component of the plasma membrane proton-loading machinery. The data in this paper identify a histidine-rich sequence within the cytoplasmic domain of the nonerythroid anion exchanger, AE2, that se...

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