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KMID : 0578319950050010020
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Molecules and Cells
1995 Volume.5 No. 1 p.20 ~ p.24
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Bovine Placental DNA Polymease δ
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Cho, Sung-Woo
Lee, Jongweon/Choi, Soo Young
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Abstract
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DNA polymerase δ was purified for the first time from bovine placenta to apparent homogeneity. DNA polymerase δ is associated with a 3´- to 5´-exonuclease activity, but it is devoid of endonuclease or 5´- to 3´-exonuclease activities. The ratios of the polymernse and exonuclease activities remained constant through the purification steps. Aphidicolin inhibited both polymerase and exonuclease activities on double-stranded DHA; However, exonuclease activity on singlestranded DNA was not inhibited. The coordinated inhibition of both polymerase and exonuclease activities of DNA polymerase δ by aphidicolin is consistent with the view that its polymerase and its exonuclease actiwities residue on the same protein molecule. DNA polymerase δ has a total molecular mass of 178 kDa and is composed of one each of 120 kDa and 52 kDa polypeptides. The enzylne is stimulated by proliferating cell nuclear antigen to 50-fold. Other biochemical properties of the enzyme were also investigated and compared to those obtained from other sources.
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KEYWORD
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