Abstract
Abstract The effects of binding phosphorylcholine to the myeloma proteins TEPC 15 and McPC 603 and their monovalent fragments, Fab', have been evaluated by fluorescence, polarization of fluorescence, difference absorption, and circular dichroism. Changes in all of these parameters are observed with TEPC 15 Fab' and in several with McPC 603 Fab'. These parameters measure various properties of the aromatic chromophores belonging to the amino acid residues tryptophan and tyrosine. Since these residues can also be located in the antibody binding site, perturbation experiments have been made. In addition, a decrease in relaxation time of TEPC 15 Fab' has been observed with ligand binding. Fluorescent data also suggest that changes in energy transfer between aromatic residues occur with phosphorylcholine binding. Taken together, the data indicate that a small structural change is produced in the monovalent antibody molecules.
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