Monoclonal antibodies as probes for monitoring the denaturation process of bovine β-lactoglobulin

摘要: Abstract Five monoclonal antibodies (MAbs) of different idiotypes were produced against bovine β-lactoglobulin (β-LG). Among them, MAbs 61B4 and 62A6 reacted preferentially to native β-LG, while 21B3 31A4 more strongly the reduced carboxymethylated (denatured) β-LG than material. These two types MAb used analyze denaturation process a molecule during heating. The binding affinity with was increased by increasing heating temperature, transition temperature being 67–68°C, that this about 80°C. Epitopes recognized shown be included in segments, Lys8-Trp19 (mostly random-coil region) Thr125-Lys135 (helical region), respectively. heat-induced conformational change is, therefore, likely start region as Lys8-Trp19, followed structural helical Thr125-Lys135. This study demonstrates is useful probe monitor local changes protein denaturation.