Human and rabbit erythrocyte membranes prepared by hypotonic hemolysis contained 5 to 15% of the phosphofructokinase in the erythrocytes. The membrane bound phosphofructokinase can be eluted by a saline wash. Human erythrocyte and rabbit muscle phosphofructokinase bind to the saline-washed membranes. This binding is specific for the inner surface of the membrane. The amount of phosphofructokinase bound is dependent on pH; at pH 7, 6 times more enzyme is bound than at pH 7.5. Unlike free phosphofructokinase, the membrane bound phosphofructokinase is not inhibited by ATP or 2,3 diphosphoglycerate and its fructose 6 P saturation curve is nonsigmoidal.
|Original language||English (US)|
|Number of pages||3|
|Journal||Journal of Biological Chemistry|
|Publication status||Published - 1977|
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