and the non specific binding of radiolabel to the antibody molecule.
We investigated both nonisotopically labelled peptides, comparing specific binding to PS and deiodination of the radiolabel in vivo.
Furthermore, the specific binding of the immunoconjugate preparations with hEGFR was comparable following radiolabeling with 111In.
The immunoconjugate was found to be stable with respect to loss of the radiolabel in vitro and immunoreactivity assays demonstrated that conjugation, radiolabeling and purification chemistries do not compromise the binding affinity or specificity for the HER2/neu antigen.
We found significant incorporation of the radiolabel into cellular macromolecules.
If the loss of radioactivity reflected unstable attachment of radiolabel to nanoparticles in vivo, we would expect the elimination curves to be governed by two kinetic processes (first, liberation of the radiolabel, and, second, brain clearance of the liberated radiolabel).
Subsequently, the appearance of the radiolabel in the circulation was monitored.
Incorporation of the radiolabel into the peptide was monitored by autoradiography.
The final incorporation of the radiolabel was approximately 1 × 108 cpm per reaction.
The incorporation of the radiolabel was analyzed with a phosphorimager as described above.
