A unique method for antibody to possess the catalytic function (3rd report)

Since a natural catalytic antibody found at 1989, many mouse- and human-type of catalytic antibodies cleaving the targeting antigens such as peptides, nucleotides, viruses and bacterial proteins, molecules such as factor VIII, CCR5, TNFα etc. have been produced so far (1, 2). In contrast, thousands of monoclonal antibodies (mAbs) have been produced over past 40 years. However, not all monoclonal antibodies have catalytic activity. It is considered that the proportion possessing a catalytic function is about several percentages or lower. Thus, the authors have continued to explore the technology how to put the catalytic function to those normal (non-catalytic) mAbs. Recently, we have made a significant progress in part with respect to the technology. After the genes of human antibody light chain were inserted into pET20b (+), E. coli was transformed and each gene was expressed by inducing with IPTG. After recovering the soluble fraction of the culture supernatant, it was purified by Ni-NTA-, cation-, and/o...