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- W45880961 abstract "A new DNA-dependent ATPase was isolated and purified from soluble extracts of Escherichia coli. This enzyme, called ATPase II, has a molecular weight of 86,000 and exists in a monomeric state. It degrades ATP (or dATP) to ADP (or dADP) and Pi in the presence of magnesium and requires a double-stranded polynucleotide as cofactor. A correlation between the efficiency as cofactor and the melting point of the polynucleotide has been found; the lower the melting temperature, the higher the stimulation of ATPase II. The enzyme binds to single-stranded DNA and poly[d(A-T)] copolymer, but not to the double-stranded circular DNA (Form I) of simian virus 40." @default.
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- W45880961 date "1978-10-01" @default.
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- W45880961 title "Purification and characterization of DNA-dependent ATPase II from Escherichia coli." @default.
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- W45880961 doi "https://doi.org/10.1016/s0021-9258(17)34529-5" @default.
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