AbstractThe anion transport system of the human erythrocyte membrane was reconstituted in unilamellar phosphatidylcholine vesicles, and a vesicle subpopulation of a narrow size distribution was isolated from the sample by gel filtration. In this subpopulation, the turnover number of the transport protein (the band 3 protein) for sulfate transport was determined. It was found that, in the reconstituted system, the protein transports sulfate 5–10-times faster than in the human erythrocyte membrane
AbstractSulfate transport by band-3 protein in adult human erythrocytes was shown to be modulated by...
AbstractThe reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte me...
The reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte membrane a...
AbstractThe anion transport system of the human erythrocyte membrane was reconstituted in unilamella...
Human erythrocyte band 3 was purified essentially free of peripheral proteins, in particular band 4....
Human erythrocyte band 3 protein was purified in 0.1% Triton X-100 and reconstituted into pre-formed...
The anion transport protein of the human erythrocyte membrane, band 3, was solubilized and purified ...
AbstractThe anion transport protein of the human erythrocyte membrane, band 3, was incorporated into...
The anion transport protein of the human erythrocyte membrane, band 3, was incorporated into unilame...
The pH dependence of sulfate transport through the red cell membranes of ten mammalian (nucleated an...
Lipid bilayer experiments were performed in the presence of solubilized band 3 protein from human re...
The paper reviews existing evidence for the participation of the protein in band 3 (nomenclature of ...
AbstractHuman erythrocyte band 3 protein was purified in 0.1% Triton X-100 and reconstituted into pr...
All cells require inorganic sulfate for normal function. Sulfate is among the most important macronu...
Vesicles have been prepared from 18 : 1c/18 : 1c-phosphatidylcholine with or without purified glycop...
AbstractSulfate transport by band-3 protein in adult human erythrocytes was shown to be modulated by...
AbstractThe reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte me...
The reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte membrane a...
AbstractThe anion transport system of the human erythrocyte membrane was reconstituted in unilamella...
Human erythrocyte band 3 was purified essentially free of peripheral proteins, in particular band 4....
Human erythrocyte band 3 protein was purified in 0.1% Triton X-100 and reconstituted into pre-formed...
The anion transport protein of the human erythrocyte membrane, band 3, was solubilized and purified ...
AbstractThe anion transport protein of the human erythrocyte membrane, band 3, was incorporated into...
The anion transport protein of the human erythrocyte membrane, band 3, was incorporated into unilame...
The pH dependence of sulfate transport through the red cell membranes of ten mammalian (nucleated an...
Lipid bilayer experiments were performed in the presence of solubilized band 3 protein from human re...
The paper reviews existing evidence for the participation of the protein in band 3 (nomenclature of ...
AbstractHuman erythrocyte band 3 protein was purified in 0.1% Triton X-100 and reconstituted into pr...
All cells require inorganic sulfate for normal function. Sulfate is among the most important macronu...
Vesicles have been prepared from 18 : 1c/18 : 1c-phosphatidylcholine with or without purified glycop...
AbstractSulfate transport by band-3 protein in adult human erythrocytes was shown to be modulated by...
AbstractThe reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte me...
The reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte membrane a...