Probing DNA polymerase alpha with monoclonal antibodies.

Zahradka P
FEBS letters (1987), Volume 212, Page 259
PubMed entry

Abstract:

DNA polymerase alpha was purified from human KB cells by ...
DNA polymerase alpha was purified from human KB cells by immunoaffinity chromatography. Enzyme activity was inhibited by three different monoclonal antibodies (SJK-132, SJK-211, SJK-287). Kinetic analysis showed that each antibody neutralized polymerase activity by a different mechanism. SJK-132 was competitive with DNA indicating it interacts with the DNA binding domain of the polymerase. SJK-287 showed a biphasic response to dCTP suggesting two dCTP binding sites exist on polymerase alpha. SJK-211 was non-competitive with DNA, dCTP and dATP.

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