Catalytically active antibodies, abzymes, appear in the blood of mammals immunized with the analogs of transition state or in the case of autoimmune diseases. Until recently, it was not shown whether abzymes exist in the blood of apparently healthy subjects. We have discovered that secretory IgA (sIgA) from the milk of healthy mothers catalyze phosphorylation of a variety of proteins and that IgG can hydrolyze DNA and RNA. In this study for the first time it is shown that IgG from human milk (and their Fab-fragments) also catalyze hydrolysis of nucleoside mono-, di-, and triphosphates. The data meet certain stringent criteria, unambiguously indicating that the observed catalytic activity is associated with IgG rather than contaminating enzymes. Although the nucleotide-binding site of IgG is located in the light antibody chain, L-chains per se cannot hydrolyze NTP unlike the DNA-hydrolyzing abzymes. Kinetic and thermodynamic parameters that characterize the interaction of NTP and dNTP with IgG-abzymes were analyzed. Possible reasons for appearance of polyclonal abzymes with different catalytic activities in the milk of healthy mothers are considered.