Abstract
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) |
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Pages (from-to) | 7418-7420 |
Number of pages | 3 |
Journal | Journal of Biological Chemistry |
Volume | 252 |
Issue number | 21 |
State | Published - 1977 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology