Abstract
Studies on structure of human erythrocyte phosphofructokinase.
Highlights
Human erythrocyte phosphofructokinase has been purified to homogeneity and some of its physicochemical properties have been investigated
Human erythrocyte phosphofructokinase has been purified to homogeneity with specific activities of approximately 97 and 135 units/mg when protein was estimated by the Lowry phenol reagent [11] and 290 nm absorption respectively, in a 40 to 50% yield based on several batches of preparation
Our purified enzyme is a large aggregate with a sedimentation coefficient of about 57 S (Fig. 1) at a protein concentration of 3 mg/ml
Summary
Human erythrocyte phosphofructokinase has been purified to homogeneity and some of its physicochemical properties have been investigated. At high protein concentrations (3 mglml), the predominant form of the enzyme shows a sedimentation coefficient of 57 S. Phosphofructokinase dissociates in 6 M guanidinium/HCl to a subunit whose molecular weight is 80,000 as determined by high speed sedimentation equilibrium. Polyacrylamide gel electrophoresis in sodium dodecyl sulfate, reveals two protein bands whose molecular weights are 80,000 and. The 85,000-dalton subunit is similar to the single subunit which occurs in human muscle phosphofructokinase. The 80,000-dalton subunit is designated as human erythrocyte enzyme subunit. One has a polyhedronal shape which is probably an aggregate of erythrocyte type of subunits. The other aggregate form, which is similar to those of human and rabbit muscle phosphofructokinases, is suggested to be the polymers of muscle type subunits of human erythrocyte phosphofructokinase
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