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Properties of an intracisternal A-particle-associated endonuclease activity which is stimulated by ATP.

机译:ATP刺激的脑内粒子相关内切核酸酶活性的性质。

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An endonuclease activity associated with purified proteinase K-treated intracisternal A-particles was identified and characterized. The activity required divalent cations, preferring Mn2+ to Mg2+. Salt concentrations above 50 mM inhibited the activity. The endonuclease was greatly stimulated by ATP, ADP, and dATP, whereas AMP appeared to produce a slight inhibition. GTP had no apparent effect on the activity. The enzyme introduced single-stranded nicks into DNA and nicked preferentially supercoiled DNA duplexes in the presence of ATP, although linear duplexes also functioned as substrates. Single-stranded DNA was not nicked to any great extent. The molecular weight of the enzyme was estimated to be about 40,000. The characteristics of this enzyme are very similar to those of the endonuclease found associated with Friend murine leukemia virus.
机译:鉴定并表征了与纯化的蛋白酶K处理的脑内α-颗粒相关的内切核酸酶活性。该活性所需的二价阳离子,优选Mn2 +至Mg2 +。 50 mm高于50mM的盐浓度抑制了活性。通过ATP,ADP和DATP大量刺激内切核酸酶,而AMP似乎产生轻微的抑制作用。 GTP对活动没有明显影响。酶将单链缺口引入DNA,并在ATP的存在下在ATP的存在下释放优先超基DNA双链体,但是线性双链体也用作基板。单链DNA未在很大程度上缩短。酶的分子量估计为约40,000。该酶的特征与与朋友鼠白血病病毒相关的内切核酸酶的特征非常相似。

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