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Phosphofructokinase from rabbit muscle was inactivated by EDTA. The inactivation rate followed first-order kinetics with respect to EDTA concentration, indicating that one enzyme subunit is modified by two moles of the chelator. The EDTA-modified protein had a lower activity than that of the native enzyme. Molecular sieve chromatography of the enzyme-EDTA complex resulted in separation of three protein species with the same mobility as the native enzyme, two EDTA-inactivated forms and one EDTA-modified form. When the amount of EDTA added was in the molar range that was associated with the inactivation, protein conformations in native and EDTA-modified enzyme were indistinguishable. However, when the molar excess of EDTA exceeded the stoichiometric amount of bound metal ion, the EDTA-modified enzyme conformation differed significantly from that of the native enzyme. The major changes observed in the EDTA-modified enzyme were a reduction in thermal stability and a decrease in gel mobility, with the conformation of the protein remaining unchanged. Methylation of the C-terminal amino group of the enzyme and proteolytic cleavage of the N-terminal amino acid residue resulted in the modification of the protein to a form of lower molecular weight, identical to that of the inactivated enzyme. Amino acid analysis of the modified enzyme revealed that the N-terminal amino group was modified, and that the C-terminal amino acid was truncated by 30 carboxyamino acids. These results indicate that the N-termin
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