Probing DNA polymerase α with monoclonal antibodies
- 23 February 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 212 (2) , 259-262
- https://doi.org/10.1016/0014-5793(87)81356-x
Abstract
DNA polymerase α 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 α. SJK-211 was noncompetitive with DNA, dCTP and dATP.Keywords
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