[Several enzymic properties of the DNA-polymerase alpha complexes with antibodies].


A highly specific rabbit antiserum against DNA polymerase alpha from regenerating rat liver (antigen AG 1) and an antiserum against the preparation of the enzyme proteolytic fragments possessing catalytic activity (antigen AG 2) were obtained. The enzyme neutralization test revealed that antibodies against AG 2 inhibit the DNA polymerase activity in a much stronger degree, than those against AG 1. Data from a kinetic analysis of the enzyme complexed with the antibodies against AG 1 suggest that the catalytic and binding sites for dNTP and free Mg2+ are altered. The value of apparent Km for activated DNA is unchanged in the DNA polymerase complexes with antibodies both against AG 1 and AG 2.




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