The anion transport protein of the human erythrocyte membrane, band 3, was incorporated into unilamellar sphingomyelin vesicles. The vesicles showed a rapid sulfate efflux which could be inhibited by specific inhibitors of the erythrocyte anion transport system. All band 3 molecules contributing to the inhibitor-sensitive flux component were arranged 'right-side-out'. The turnover number of the transport protein for sulfate transport was virtually identical to that in phosphatidylcholine bilayers and around 6 times larger than in human erythrocyte membranes. Thus, in contrast to other claims, sphingomyelin does not inhibit the erythrocyte anion transport system
Anion transport in the trout red blood cell is mediated by a membrane protein that selectively binds...
The reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte membrane a...
Effects of anion transport inhibitors on hemolysis of human erythrocytes at 200 MPa were examined. T...
AbstractThe anion transport protein of the human erythrocyte membrane, band 3, was incorporated into...
Human erythrocyte band 3 was purified essentially free of peripheral proteins, in particular band 4....
AbstractThe anion transport system of the human erythrocyte membrane was reconstituted in unilamella...
Sphingomyelin is a major lipid of the mammalian cell surface. The view that sphingomyelin, after syn...
Band 3 protein of the human erythrocyte membrane, the anion transport protein, possesses a high affi...
Mono‐, di‐, and trisulfonic acids, including 4,4′‐diacetamido stilbene‐2,2′‐disulfonic acid (DAS) an...
Sphingosine 1-phosphate (S1P) is a bioactive lipid mediator that is thought to be involved in variou...
<div><p>Sphingosine 1-phosphate (S1P) is a bioactive lipid mediator that is thought to be involved i...
The anion transport protein of the human erythrocyte membrane, band 3, was solubilized and purified ...
Hereditary spherocytosis (HS) is due to different membrane protein defects (i.e., deficiency of spec...
AbstractThe reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte me...
The disulfonic acid APMB produces maximally about 85% inhibition of sulfate equilibrium exchange. In...
Anion transport in the trout red blood cell is mediated by a membrane protein that selectively binds...
The reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte membrane a...
Effects of anion transport inhibitors on hemolysis of human erythrocytes at 200 MPa were examined. T...
AbstractThe anion transport protein of the human erythrocyte membrane, band 3, was incorporated into...
Human erythrocyte band 3 was purified essentially free of peripheral proteins, in particular band 4....
AbstractThe anion transport system of the human erythrocyte membrane was reconstituted in unilamella...
Sphingomyelin is a major lipid of the mammalian cell surface. The view that sphingomyelin, after syn...
Band 3 protein of the human erythrocyte membrane, the anion transport protein, possesses a high affi...
Mono‐, di‐, and trisulfonic acids, including 4,4′‐diacetamido stilbene‐2,2′‐disulfonic acid (DAS) an...
Sphingosine 1-phosphate (S1P) is a bioactive lipid mediator that is thought to be involved in variou...
<div><p>Sphingosine 1-phosphate (S1P) is a bioactive lipid mediator that is thought to be involved i...
The anion transport protein of the human erythrocyte membrane, band 3, was solubilized and purified ...
Hereditary spherocytosis (HS) is due to different membrane protein defects (i.e., deficiency of spec...
AbstractThe reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte me...
The disulfonic acid APMB produces maximally about 85% inhibition of sulfate equilibrium exchange. In...
Anion transport in the trout red blood cell is mediated by a membrane protein that selectively binds...
The reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte membrane a...
Effects of anion transport inhibitors on hemolysis of human erythrocytes at 200 MPa were examined. T...