Cooperative association of plasminogen with fibrinogen.
We have examined the association of both Glu- and Lys-plasminogen to fibrinogen by ultracentrifugal sedimentation equilibrium in neutral isotonic buffer in the presence of aprotinin. The fibrinogen and plasminogens, which were homogenous, did not exhibit any self-association. In each association study, five different molar ratios of plasminogen to fibrinogen were examined. The data were analyzed by mathematical modeling using nonlinear least-squares curve fitting. Analyses of molecular species present showed that up to 4 mol of either Glu- or Lys-plasminogen was associated with each mol of fibrinogen. For the binding of Glu-plasminogen, the values of the successive changes of the standard free energy of association were found to be -5.48, -7.73, -8.88, and -11.41 kcal/mol (Ka = 2.16 X 10(4), 1.32 X 10(6), 1.06 X 10(7), and 1.08 X 10(9) M-1). For the experimental conditions used here, the association of Lys-plasminogen appears to be described by virtually the same fitting parameters. The very marked cooperativity of association found here would appear to imply that there are significant alterations of the structure of fibrinogen as a result of each successive molecule of plasminogen bound.
D001665:Binding Sites; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D008433:Mathematics; D010446:Peptide Fragments / Q000378:metabolism; D010958:Plasminogen / Q000378:metabolism*; D011485:Protein Binding; D013816:Thermodynamics
D010446:Peptide Fragments; C018998:lysyl-plasminogen; D005340:Fibrinogen; D010958:Plasminogen