Abstract
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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