Evidence against the Involvement of Mutarotase in the D-Glucose Uptake Activity of Isolated Human Erythrocyte Membranes
1972 ◽
Vol 50
(9)
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pp. 1028-1030
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Keyword(s):
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.
1972 ◽
Vol 247
(14)
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pp. 4572-4576
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1972 ◽
Vol 247
(4)
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pp. 1156-1160
Keyword(s):
1982 ◽
pp. 263-266
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The stereospecific d-glucose transport activity of cholate extracts from human erythrocyte membranes
1981 ◽
Vol 644
(1)
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pp. 101-107
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1981 ◽
Vol 648
(2)
◽
pp. 254-262
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1995 ◽
Vol 5
(8)
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pp. 827-830
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Keyword(s):
1975 ◽
Vol 250
(9)
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pp. 3217-3220
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