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Probing DNA polymerase α with monoclonal antibodies
Author(s) -
Zahradka Peter
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81356-x
Subject(s) - monoclonal antibody , polymerase , microbiology and biotechnology , dna polymerase , dna , virology , chemistry , antibody , biology , genetics , biochemistry
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.