Purification of human erythrocyte phosphofructokinase
نویسندگان
چکیده
منابع مشابه
Studies on structure of human erythrocyte phosphofructokinase.
Human erythrocyte phosphofructokinase has been purified to homogeneity and some of its physicochemical properties have been investigated. The enzyme exists in several polymeric states. At high protein concentrations (3 mglml), the predominant form of the enzyme shows a sedimentation coefficient of 57 S. In highly dilute solution (0.3 to 10 pg/ ml), the enzyme is in 12 S to 18 S forms as shown b...
متن کاملWith Erythrocyte Phosphofructokinase Deficiency
Hereditary nonspherocytic hemolysis sitivity to adenosine triphosphate inhiassociated with abnormal erythrocyte bition. Erythrocyte adenosine triphosphosphofructokinase activity was dephate levels were depressed. The monstrated in a young man. Enzyme absence of muscle disease and the activity in the propositus, his mother, presence of normal in vivo lactate and maternal grandmother was approxpr...
متن کاملPurification of Human Erythrocyte Pyruvate ICinase*
We describe a purification scheme for human erythrocyte pyruvate kinase. Following two ammonium sulfate fractionations, batchwise absorption on CM-cellulose, chromatography on CM-cellulose with fructose 1,6-diphosphate elution, and chromatography on DEAE-cellulose, a 30,000fold purification was achieved with a yield of 8% from the original hemolysate. Antiserum against partially purified pyruva...
متن کاملPurification of human erythrocyte pyruvate kinase.
We describe a purification scheme for human erythrocyte pyruvate kinase. Following two ammonium sulfate fractionations, batchwise absorption on CM-cellulose, chromatography on CM-cellulose with fructose 1,6-diphosphate elution, and chromatography on DEAE-cellulose, a 30,000fold purification was achieved with a yield of 8% from the original hemolysate. Antiserum against partially purified pyruva...
متن کاملThe interaction of phosphofructokinase with erythrocyte membranes.
The interaction of muscle phosphofructokinase with human erythrocyte ghost membranes was investigated. Scatchard analysis of the binding reveals only a single class of binding sites numbering approximately 4 x 10” sites/ghost with an association constant of 2 X lo7 M-‘. Maximum binding is observed below pH 6.8 and is complete within 30 min at 4”, 24”, and 37°C; binding is inhibited by high ioni...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1972
ISSN: 0014-5793
DOI: 10.1016/0014-5793(72)80060-7