Hachmann H J, Lezius A G
Eur J Biochem. 1976 Jan 15;61(2):325-30. doi: 10.1111/j.1432-1033.1976.tb10025.x.
An ATPase was purified from mouse myeloma MOPC 70E the activity of which depends on the presence of single-stranded DNA and divalent cations such as Mg2+, Mn2+, Ca2+, Ni2+ or Fe2+. The enzyme splits both ribonucleoside and deoxyribonucleoside triphosphates but preferentially ATP and dATP yielding nucleoside diphosphates and inorganic phosphate. The enzyme has an absolute requirement for single-stranded DNA. Alternating double-stranded polydeoxynucleotides are only slight effective, and native double-stranded DNA, single-stranded and double-stranded RNAs as well as DNA - RNA hybrids are ineffective in stimulating the ATPase. The enzyme has further characterized by sedimentation in a sucrose density gradient (s20, w = 5.5 S) and by isoelectric focussing in an ampholine pH gradient (pI = 6.5).
从鼠骨髓瘤MOPC 70E中纯化出一种ATP酶，其活性依赖于单链DNA以及二价阳离子（如Mg2+、Mn2+、Ca2+、Ni2+或Fe2+）的存在。该酶能水解核糖核苷三磷酸和脱氧核糖核苷三磷酸，但优先作用于ATP和dATP，生成核苷二磷酸和无机磷酸。该酶对单链DNA有绝对需求。交替的双链多脱氧核苷酸仅有轻微作用，而天然双链DNA、单链和双链RNA以及DNA-RNA杂交体在刺激ATP酶方面均无作用。该酶通过在蔗糖密度梯度中的沉降（s20,w = 5.5 S）以及在两性电解质pH梯度中的等电聚焦（pI = 6.5）进一步得以表征。
