Yaginuma K, Koike K
Nucleic Acids Res. 1981 Apr 24;9(8):1949-61. doi: 10.1093/nar/9.8.1949.
A DNA-dependent ATPase has been highly purified from rat liver mitochondria and characterized. The enzyme catalyzes the hydrolysis of ATP or dATP in the presence of single-stranded DNA cofactor and a divalent cation. The Km values for ATP and dATP are 0.15 mM and 0.35 mM, respectively. The enzyme activity is highly sensitive to N-ethylmaleimide. The sedimentation coefficient of the enzyme is 8.3 S in a glycerol gradient. From this and data on Sephadex G-200 gel filtration, the molecular weight of the native enzyme was calculated to be about 190,000. All the natural single-stranded DNAs tested were equally effective for the ATPase activity, but synthetic deoxyhomopolymer poly(dC) was found to be more effective than natural single-stranded DNAs. Synthetic and natural RNAs had no effect on the activity.
一种依赖DNA的ATP酶已从大鼠肝脏线粒体中高度纯化并进行了特性鉴定。该酶在单链DNA辅因子和二价阳离子存在的情况下催化ATP或dATP的水解。ATP和dATP的米氏常数分别为0.15 mM和0.35 mM。该酶活性对N - 乙基马来酰亚胺高度敏感。在甘油梯度中该酶的沉降系数为8.3 S。根据此数据以及在Sephadex G - 200凝胶过滤中的数据，计算出天然酶的分子量约为190,000。所有测试的天然单链DNA对ATP酶活性的作用相同，但发现合成的脱氧同聚物聚（dC）比天然单链DNA更有效。合成RNA和天然RNA对该活性均无影响。
