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Human acute myeloblast leukemia HL60 cells overexpresses a beta - type DNA polymerase (EC 2.7.7.7) which is found to be operated by magnetic isotope effect (MIE) of Calcium once the Mg^(2+) ions replaced with the stable ^(43)Ca^(2+) isotopes inside the enzyme catalytic sites. The isotopes mentioned are the only paramagnetic species of the Calcium isotopic set with a 0.135 natural abundance value and the negative 7/2 nuclear spin providing a nuclear magnetic moment equal to 1.317 Bohr magnetons. As compared to the Mg/^(40)Ca substitution, a 2.25-fold enzyme inhibition has been shown to prove the ^(43)Ca-MIE dependent mode of the catalysis turning down. This ^(43)Capromoted enzyme hyper-suppression leads to a residual synthesis of shorted DNA fragments that counts 25-35 nucleotides in length contrasting with the 180 n-210 n DNA produced by either intact or ^(40)Ca-loaded polymerase. Being occurred simultaneously with a marked MIE-promoted enzyme inhibition, this fact itself makes possible to consider these short (size-invalid) DNA segments hardly efficient in the DNA base-excision repair. The latter is a survival factor in leukemic cells where the DNApolβ was found over expressed. That confirms a concept considering the DNApolβ a legitimate target for antitumor agents since its inhibition deprives the malignant cell from a DNA base-excision repair in neoplasma. A possible trend making role of these data for molecular pharmacology of cancers is in a focus.

The DNA Repair Key Enzyme Affected by <sup>43</sup>Ca<sup>2+</sup>: A New Platform for Anti-Leukemia Experimental Pharmacology