Results 241 to 250 of about 80,553 (266)
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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.
P K, Werner, R A, Reithmeier
openaire   +2 more sources

The anion transport protein of the red cell membrane. A zipper mechanism of anion exchange.

The Tokai journal of experimental and clinical medicine, 1983
The anion exchange system of the red cell membrane resides in an integral membrane protein with a molecular mass of approximately 10(5) daltons. We report on the identification of the transport system by means of covalently binding stilbene-disulfonates.
J O, Wieth   +3 more
openaire   +1 more source

STRUCTURE OF THE ERYTHROCYTE ANION TRANSPORT PROTEIN*

Annals of the New York Academy of Sciences, 1980
M J, Tanner, D G, Williams, R E, Jenkins
openaire   +2 more sources

STRUCTURE OF THE ERYTHROCYTE ANION TRANSPORT PROTEIN

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

Stimulus-Controlled Anion Binding and Transport by Synthetic Receptors

Chemical Reviews, 2023
Jorn De Jong   +2 more
exaly  

PROTEIN STRUCTURE IN RELATION TO ANION TRANSPORT IN RED CELLS*

Annals of the New York Academy of Sciences, 1980
A, Rothstein   +3 more
openaire   +2 more sources

Transmembrane Transport of Bicarbonate by Anion Receptors

ChemPlusChem, 2022
Luis Martínez-Crespo   +1 more
exaly  

Exploiting the Catenane Mechanical Bond Effect for Selective Halide Anion Transmembrane Transport

Angewandte Chemie - International Edition, 2023
Hui Min Tay   +2 more
exaly  

FA Sliding as the Mechanism for the ANT1-Mediated Fatty Acid Anion Transport in Lipid Bilayers

International Journal of Molecular Sciences, 2023
Jürgen Kreiter   +2 more
exaly  

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