title: Purification of F4 phosphofructokinase from human platelets and comparison with the other phosphofructokinase forms.
abstract: The phosphofructokinase (ATP:D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) tetramers F4, F3L and F2L2 have been separated from human platelets, and purified to homogeneity by affinity chromatography on Dextran Blue-Sepharose 4B. The F subunits have a molecular weight of 85 000, identical to that of the M subunits. By contrast with L-type phosphofructokinase, the F-type enzyme seems to exist predominantly in a tetrameric form and not to aggregate to high molecular weight polymers. Specific activity of pure F4 phosphofructokinase is about 140 IU/mg of protein. Immunologically, it is easy to distinguish all the basic phosphofructokinase forms (i.e. M, L and F types); nevertheless a slight immunological cross-reactivity seems to exist between all these forms.
mesh_terms: D001792:Blood Platelets / Q000201:enzymology*; D006098:Granulocytes / Q000201:enzymology; D006801:Humans; D005779:Immunodiffusion; D007527:Isoenzymes / Q000097:blood* / Q000302:isolation & purification; D007951:Leukemia, Myeloid / Q000201:enzymology; D046911:Macromolecular Substances; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D009928:Organ Specificity; D010732:Phosphofructokinase-1 / Q000097:blood* / Q000302:isolation & purification
chemical_list: D007527:Isoenzymes; D046911:Macromolecular Substances; D010732:Phosphofructokinase-1