Isolation and dynamic hapten binding properties of 2,4,6-triphenyl- N-(4-hydroxyphenyl)-pyridinium (THP-) specific antibodies from bovine colostrum—II : Characteristic differences in hapten binding kinetics of 7S and 19S anti-THP antibodies

The hapten binding properties of purified 7S and 19S 2,4,6-triphenyl- N-(4-hydroxyphenyl)-pyridinium (THP ∗-) specific antibodies were studied by temperature-jumped spectrometry. In both cases a nearly diffusion-controlled hapten-antibody recombination process in the μsec range was observed. In the case of the 19S immunoglobulins an additional relaxation process in the msec range was found to be independent of reactant concentrations. This slow first-order process, suggesting structural rearrangements of the antibodies, is discussed with respect to hapten-dependent conformational changes of the immunoglobulins.