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Description
Phosphofructokinase (PFK), a major regulatory enzyme in all cells of the body, catalyzes the metabolism of sugar, and thereby is pivotal in the production of energy to maintain normal cell function. In human there are three structural loci controlling PFK: M (muscle), L (liver), and P (platelet) type subunits, which are variably expressed in different tissues; human diploid fibroblasts and leukocytes express all three genes. PFK, a tetramer formed by the random association of the products of two separate gene loci to form the five possible tetramers. PFKs of muscle and liver are homotetramers of the M and L subunits, respectively. Red cells have all five isozymes: M4, M3L, M2L2, ML3, and L4. PFK is an allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate. PFK catalyzes the key controlling step of glycolytic pathway. PFK deficiency can present as mild to life-threatening episodic illness. A hallmark sign of this disease is intermittent dark urine, with the color of the urine ranging from orange to dark coffee-brown, which commonly develops following strenuous exercise. The mean red cell PFK is elevated in persons with Down syndrome. This PFKL antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 669-699 amino acids from the C-terminal region of human PFKL.