The presence of an exonuclease in highly purified DNA polymerase from bakers' yeast.
作者： William B. Helfman
DOI: 10.1111/J.1432-1033.1973.TB02576.X
关键词:
摘要: Two DNA polymerase activities from bakers' yeast can be separated by DEAE-cellulose chromatography, one of which dissociated its DNAase activity subsequent chromatography on phosphocellulose. Both the polymerases prefer nicked double-stranded and utilize single-stranded efficiently only at high ratios enzyme to template. is completely inhibited p-hydroxymercuribenzoate, suggesting that cysteine essential for activity. The has been shown coincident with during chromatography. This hydrolyzes preferentially, releasing deoxymononucleotides as sole product. The rate hydrolysis unaffected presence a 2′,3′-dideoxy terminus poly(dT).
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