scholarly journals Chloride binding to the anion transport binding sites of band 3. A 35Cl NMR study.

1984 ◽  
Vol 259 (10) ◽  
pp. 6472-6480
Author(s):  
J J Falke ◽  
R J Pace ◽  
S I Chan
Keyword(s):  
Binding Sites ◽  
Band 3 ◽  
Anion Transport ◽  
Chloride Binding ◽  
Nmr Study

The red cell band 3 protein: its role in anion transport

1982 ◽  
Vol 299 (1097) ◽  
pp. 497-507 ◽  
Keyword(s):  
Binding Sites ◽  
Band 3 ◽  
Anion Transport ◽  
Anion Binding ◽  
Hydrophobic Residues ◽  
Ping Pong ◽  
Hydrophilic Residues ◽  
Aqueous Core ◽  
Positively Charged

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. The kinetics are consistent with a ping-pong model in which positively charged anion-binding sites can alternate between exposure to the inside and outside compartments but can only shift one position to the other when occupied by an anion. The structural studies on band 3 indicate that only 60 % of the peptide is essential for transport. That particular portion is in the form of a dimer consisting of an assembly of membrane-crossing strands (each monomer appears to cross at least five times). The assembly presents its hydrophobic residues toward the interior of the bilayer, but its hydrophilic residues provide an aqueous core. The transport involves a small conformational change in which an anion-binding site (involving positively charged residues) can alternate between positions that are topologically in and topologically out.

Further Studies on Zn2+-Mediated Domain–Domain Communication in Human Erythrocyte Band 3

1998 ◽  
Vol 18 (5) ◽  
pp. 265-277
Author(s):  
Hong Xu ◽  
Xujia Zhang ◽  
Fu Yu Yang
Keyword(s):  
Conformational Change ◽  
Human Erythrocyte ◽  
Cytoplasmic Domain ◽  
Band 3 ◽  
Anion Transport ◽  
Intrinsic Fluorescence ◽  
Transport Activity ◽  
Membrane Domain ◽  
Nmr Study ◽  
Anion Transport Activity

Human erythrocyte band 3 is purified and reconstituted into vesicles, forming right-side-out proteoliposomes. Zn2+ entrapped inside the proteoliposomes inhibits the anion transport activity of band 3, and removal of the cytoplasmic domain of band 3 is able to diminish Zn2+ inhibition. Thus, the inhibition of activity of band 3 results from the Zn2+ induced conformational change of the cytoplasmic domain, which in turn is transmitted to the membrane domain. The results of intrinsic fluorescence and its quenching by HB and the 35Cl NMR study indicate that the cytoplasmic domain is essential for the conformational change induced by Zn2+.SH-blocking reagents, CH3I and GSSG, are used to modify the cytoplasmic domain, where they specifically bind to Cys201 and Cys317. It is observed that the Zn2+ induced inhibition of anion transport activity is blocked. This demonstrates that Cys201 and Cys317 are required in Zn2+-mediated domain–domain communication.

Inhibition of chloride binding to the anion transport site by diethylpyrocarbonate modification of band 3

1990 ◽  
Vol 116 (1) ◽  
pp. 87-91 ◽  
Author(s):  
Naotaka Hamasaki ◽  
Kenji Izuhara ◽  
Kenshi Okubo ◽  
Yoko Kanazawa ◽  
Akira Omachi ◽  
...  
Keyword(s):  
Band 3 ◽  
Anion Transport ◽  
Chloride Binding ◽  
Transport Site

A 35Cl and 37Cl NMR study of chloride binding to the erythrocyte anion transport protein

1991 ◽  
Vol 40 (3) ◽  
pp. 329-337 ◽  
Author(s):  
William S. Price ◽  
Philip W. Kuchel ◽  
Bruce A. Cornell
Keyword(s):  
Anion Transport ◽  
Transport Protein ◽  
Chloride Binding ◽  
Nmr Study

Alterations of band 3 transport protein by cellular aging and disease: erythrocyte band 3 and glucose transporter share a functional relationship

1990 ◽  
Vol 68 (12) ◽  
pp. 1419-1427 ◽  
Author(s):  
Gieljan J. C. G. M. Bosman ◽  
Marguerite M. B. Kay
Keyword(s):  
Glucose Transport ◽  
Structural Changes ◽  
Glucose Transporter ◽  
Functional Relationship ◽  
Band 3 ◽  
Anion Transport ◽  
Cellular Aging ◽  
Abnormal Band ◽  
Membrane Spanning

Structural changes in human erythrocyte band 3 that affect anion transport are correlated with changes in glucose transport in situ. Breakdown of band 3, observed during normal erythrocyte aging in situ and in some diseases involving erythrocytes, is associated with an increase in Km and a decrease in Vmax of sulfate self-exchange, and with an increase in Km and Vmax of glucose efflux. Erythrocytes containing a high molecular weight form of band 3 exhibit an increase in Vmax of sulfate exchange and a decrease in Vmax of glucose efflux. Identical transport characteristics are observed in abnormal band-3-containing erythrocytes from individuals with familial amyotrophic chorea with acanthocytosis. A third band 3 alteration, fast-aging band 3, exhibits decreased Vmax of sulfate exchange and an increase in Km and decrease in Vmax of glucose efflux. Changes in band 3 structure that are the result of unstable hemoglobin or a deficiency in glucose-6-phosphate dehydrogenase and that do not affect anion transport have no effect on glucose transport characteristics. These data indicate the existence of a functional relationship between the membrane-spanning, anion-transport domain of band 3 and glucose transport in human erythrocytes. Antibodies to synthetic peptides reveal structural changes in membranes from the three inborn band 3 alterations and in band 3 itself in membranes from fast-aging band 3. Thus, immunological data suggests a structural relationship between anion and glucose transporters.Key words: red cell, anion transport, membrane proteins, aging, choreoacanthocytosis, anemia.

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