中文摘要：

Saccharomyces cerevisiae Pif1p helicase 是从酵母被保存到人的 Pif1 亚科的成立成员。酵母 PIF1 基因的潜在的人的相当或相同的事物从 Hek293 房间线的 cDNA 图书馆被克隆。这里，我们描述了 S-transferase (GST ) 熔化了的谷胱甘肽的一个纯化过程 N 终端从酵母截断了人的 Pif1 蛋白质(hPif1deltaN ) 并且描绘了它的 ATP 水解作用活动的酶的动力学。人的 Pif1 的 ATPase 活动依赖于二价的阳离子，例如 Mg2+ ， Ca2+ 和搁浅单人赛的 DNA。为为 ATPase 活动的 ATP 的 Km 是约 200 microM。因为 ATPase 活动为 hPif1 的 helicase 活动是必要的，这些结果将在 hPif1 上便于进一步的调查。

英文摘要：

Saccharomyces cerevisiae Pif1p helicase is the founding member of the Pif1 subfamily that is conserved from yeast to human. The potential human homolog of the yeast PIF1 gene has been cloned from the cDNA library of the Hek293 cell line. Here, we described a purification procedure of glutathione Stransferase （GST）-fused N terminal truncated human Pif1 protein （hPif1AN） from yeast and characterized the enzymatic kinetics of its ATP hydrolysis activity. The ATPase activity of human Pif1 is dependent on divalent cation, such as Mg^2＋, Ca^2＋ and single-stranded DNA. Km for ATP for the ATPase activity is approximately 200 μM. As the ATPase activity is essential for hPif1＇s helicase activity, these results will facilitate the further investigation on hPif1.