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- W1964834038 abstract "Two DNA polymerase activities from bakers' yeast can be separated by DEAE-cellulose chromatography, one of which can be dissociated from its DNAase activity by subsequent chromatography on phosphocellulose. Both of the DEAE-cellulose polymerases prefer nicked double-stranded DNA and utilize single-stranded DNA efficiently only at high ratios of enzyme to template. DNA polymerase activity is completely inhibited by p-hydroxymercuribenzoate, suggesting that cysteine is essential for activity. The DNAase has been shown to be coincident with polymerase activity during chromatography. This enzyme hydrolyzes single-stranded DNA preferentially, releasing deoxymononucleotides as the sole product. The rate of hydrolysis is unaffected by the presence of a 2′,3′-dideoxy terminus on poly(dT)." @default.
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- W1964834038 date "1973-01-01" @default.
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- W1964834038 title "The Presence of an Exonuclease in Highly Purified DNA Polymerase from Bakers' Yeast" @default.
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- W1964834038 doi "https://doi.org/10.1111/j.1432-1033.1973.tb02576.x" @default.
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