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A 44 kDa C-terminal fragment of o29 DNA polymerase has been separately expressed and purified from Escherichia coli cells. As expected, the truncated protein lacked the 3'-5' exonuclease activity and strand-displacement capacity, previously mapped in the N-terminal domain of o29 DNA polymerase. On the other hand, the 44 kDa C-terminal fragment retained polymerase activity when using Mn 2+...
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