scholarly journals Partial purification of the D-glucose transport protein from human erythrocyte membranes by affinity chromatography on wheat germ lectin-sepharose

FEBS Letters ◽  
1981 ◽  
Vol 129 (1) ◽  
pp. 100-104 ◽  
Author(s):  
Gunnar Fröman ◽  
Per Lundahl ◽  
Fernando Acevedo
Biochemistry ◽  
1985 ◽  
Vol 24 (12) ◽  
pp. 2843-2848 ◽  
Author(s):  
Kimio Oikawa ◽  
Debra M. Lieberman ◽  
Reinhart A. F. Reithmeier

1972 ◽  
Vol 50 (9) ◽  
pp. 1028-1030 ◽  
Author(s):  
Arthur Kahlenberg ◽  
Gary Miller

Mutarotase, the enzyme catalyzing the interconversion of the anomeric forms of D-glucose, has recently been suggested to be the membrane glucose carrier in human erythrocytes. However, hemoglobin-free human erythrocyte membranes possessing D-glucose uptake activity were found to be free of mutarotase activity. Mutarotase activity was detected in the membrane-free hemolysates of the cells. It is therefore concluded that the D-glucose uptake activity of isolated erythrocyte membranes is not due to the binding of the sugar to mutarotase, and that this enzyme is not involved in glucose transport in a manner compatible with most presently held concepts of the membrane transport process.


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