The recognition domain for the low density lipoprotein cellular receptor is expressed once on each lipoprotein particle.

The stoichiometry of binding of monoclonal antibodies and Fab fragments to LDL was assessed. Increasing amounts of two [125I]-labelled antibodies which define epitopes at or near the LDL-receptor recognition domains of apoB were incubated with fixed amounts of LDL and antibody-LDL complexes were separated from free antibodies by heparin-MnCl2 precipitation. Saturation kinetics were obtained and data were analyzed according to Scatchard. One antibody or Fab fragment was bound per LDL particle. Homogeneity of binding was indicated by straight Scatchard lines and by the binding of virtually all LDL particles by an antibody affinity chromatographic column.