Phospholipid dependence of the anion transport system of the human erythrocyte membrane. Studies on reconstituted band 3/lipid vesicles

1983 ◽  
Vol 730 (1) ◽  
pp. 139-150 ◽  
Author(s):  
W. Köhne ◽  
B. Deuticke ◽  
C.W.M. Haest
Keyword(s):  
Erythrocyte Membrane ◽  
Transport System ◽  
Human Erythrocyte ◽  
Lipid Vesicles ◽  
Band 3 ◽  
Anion Transport ◽  
Human Erythrocyte Membrane ◽  
Anion Transport System

scholarly journals The aldolase-binding site of the human erythrocyte membrane is at the NH2 terminus of band 3.

1981 ◽  
Vol 256 (21) ◽  
pp. 11203-11208 ◽  
Author(s):  
S.N. Murthy ◽  
T. Liu ◽  
R.K. Kaul ◽  
H. Köhler ◽  
T.L. Steck
Keyword(s):  
Binding Site ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Human Erythrocyte Membrane

scholarly journals The interaction of 3-deoxy-3-fluoro-d-glucose with the hexose-transport system of the human erythrocyte

1973 ◽  
Vol 135 (4) ◽  
pp. 773-777 ◽  
Author(s):  
G. J. Riley ◽  
N. F. Taylor
Keyword(s):  
Kinetic Parameters ◽  
Erythrocyte Membrane ◽  
Transport System ◽  
Dissociation Energy ◽  
Human Erythrocyte ◽  
Optical Method ◽  
Hexose Transport ◽  
Human Erythrocyte Membrane ◽  
Significant Release ◽  
Glucose Carrier

1. By using an optical method the kinetic parameters of hexose transport across the human erythrocyte membrane were determined for several sugars. The series of half-saturated constants is as follows: 3-deoxy-3-fluoro-d-glucose = 3-O-methyl-d-glucose <d-glucose<d-mannose <3-deoxy-d-glucose<d-galactose<l-arabinose. 2. Estimations of the dissociation energy of the 3-deoxy-3-fluoro-d-glucose–carrier and d-glucose–carrier complexes suggest that the binding of the two sugars to the transport system is equivalent. 3. Incubation of the erythrocytes with 3-deoxy-3-fluoro-d-glucose results in a small but significant release of F−anion. Cells treated in this way lose their ability to transport glucose.

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