Monoclonal antibodies assisting refolding of firefly luciferase.

The reactivation efficiency in the refolding of denatured luciferase in the presence and the absence of monoclonal antibodies (mAbs) has been studied. Luciferase could be partially reactivated when the protein was denatured in high concentrations of guanidium chloride (GdmCl; >4.5 M) and the refolding was carried out in very low protein concentrations.

The Preparation of the Antigen Conformation-related Monoclonal Antibodies against Maltose-Binding Protein.

Making use of the high expression efficiency of maltose-binding protein (MBP) in E. coli, the soluble and the inclusion body forms of MBP were purified to homogeneity by affinity chromatography and by denaturation, refolding and gel filtration respectively. After immunized Balb/C mice with two forms of MBP respectively, 5 clones for each antigen form were found to secrete monoclonal antibodies.