By immunizing ground-state peptides or proteins, we can produce super catalytic antibodies possessing serine protease-like characteristics. The unique feature of super catalytic antibodies is their ability to decompose a target molecule that is being killed. The authors have succeeded in preparing super catalytic antibodies that destroy (i) the HIV-1 envelope protein gp41, (ii) chemokine receptor CCR5 peptide, and (iii) Helicobacter pylori urease, etc. Some of them can degrade antigens at high catalytic reaction rates. Regarding their K-m and k(cat), super catalytic antibodies show intermediary values between that of enzymes (high K-m and k(cat)) and that of antibodies (low K-m and k(cat) [ = 0]). The catalytic function of an antibody mostly resides in its light chain. From mouse Vkappa germline analysis, it became clear that super catalytic antibodies are generated from some discrete germlines such as bb1, cr1, cs1, bl1, bj2 and bd2. In these Vkappa germlines, at least one catalytic triad composed of three amino acid residues, namely, Asp1, Ser27a and His93, is encoded. Namely, the antibody light chains (super catalytic antibodies) generated from the germlines are inherently able to enzymatically decompose antigens. Thus, such antibody light chains can be referred to as antigenase (antigen-decomposing enzyme) and may have arisen during the evolution of antibodies to acquire a higher ability than that of enzymes for developing a sophisticated self-defense system for survival.