中文摘要：

Aeropyrum pernix 包含 ribonuclease H (RNase H ) 的一个相当或相同的事物，一。pernix RNase HII (Ape-RNase HII ) 。活动描述证明 Ape-RNase HII 面对 5 公里 Mn2+ ， 1 公里 Co2+ ，或 10 公里展出了最高的活动 Mg2+ 分别地；然而，它在为 Mn2+ 和 Mg2+ 的不同劈开地点的劈开效率是不同的。Ape-RNase HII 在多重地点劈开 12-bp RNA/DNA 底层，最佳 pH 价值是 11.0。而且， 16-bp DNA-r4-DNA/DNA 和 13-bp DNA-r1-DNA/DNA 妄想的底层在 DNARNA 被劈开连接。Ape-RNase HII 是 thermostable，稳定与增加的盐集中被提高。这个工作被相信在 Ape-RNase HII 和结果的功能的学习应该贡献的 vitro 是第一另外的 archaeal 种类的 RNase H 的分析。

英文摘要：

Aeropyrum pernix contains one homolog of ribonuclease H （RNase H）, A. pernix RNase HII （Ape-RNase HII）. Activity characterization showed that Ape-RNase HII exhibited the highest activity in the presence of 5 mM Mn^2＋, l mM Co^2＋, or 10mM Mg^2＋, respectively; however, its cleavage efficiencies at different cleavage sites for Mn^2＋ and Mg^2＋ were different. Ape-RNase HII cleaved 12-bp RNA/DNA substrates at multiple sites and the optimum pH value was 11.0. Moreover, 16-bp DNA- r4-DNA/DNA and 13-bp DNA-rl-DNA/DNA chimeric substrates were cleaved at DNA-RNA junction. Ape- RNase HII was thermostable and the stabilization was enhanced with increased salt concentration. This work is believed to be the first in vitro functional study of Ape- RNase HII and the results should contribute to the ana- lysis of RNase H of other archaeal species.