scholarly journals Hydroxyapatite chromatography of the D-glucose transport protein of human erythrocyte membranes

FEBS Letters ◽  
1982 ◽  
Vol 143 (2) ◽  
pp. 220-224 ◽  
Author(s):  
Gunnar Fröman
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.


Biochemistry ◽  
2005 ◽  
Vol 44 (15) ◽  
pp. 5606-5616 ◽  
Author(s):  
Kara B. Levine ◽  
Trista K. Robichaud ◽  
Stephanie Hamill ◽  
Lisa A. Sultzman ◽  
Anthony Carruthers

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