A monoclonal antibody against purified calf DNA polymerase α (deoxynucleosidetriphosphate:DNA deoxy-nucleotidyltransferase, EC 184.108.40.206) was used to immunoprecipitate proteins from a crude soluble extract of growing monkey BSC-1 cells. Immunoprecipitates contained familiar DNA polymerase α catalytic polypeptides of M(r)S ≃ 115,000 and 70,000 and also a M(r) 40,000 catalytic polypeptide; the major component in the immunoprecipitates, however, was a polypeptide M(r) ≃ 190,000 not previously identified as a DNA polymerase. This protein was capable of DNA polymerase activity after electroelution from NaDodSO4/polyacrylamide gels and renaturation. The highly purified enzyme so obtained was active with poly(dT)·oligo(rA) as template·primer, resistant to dideoxy TTP (ddTTP), and inhibited by aphidicolin and butylphenyldeoxyguanosine 5'-triphosphate, thus identifying it as a DNA polymerase α. The results indicate that a polypeptide of M(r) ≃ 190,000 is an abundant component among DNA polymerase α catalytic polypeptides in growing monkey cells.
|Original language||English (US)|
|Number of pages||5|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|Issue number||24 I|
|State||Published - 1984|
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