XPG蛋白具有结构特异性核酸内切酶活性。
XPG protein has a structure-specific endonuclease activity.
作者信息
Cloud K G, Shen B, Strniste G F, Park M S
机构信息
Life Sciences Division, Los Alamos National Laboratory, NM 87545, USA.
出版信息
Mutat Res. 1995 Jul;347(2):55-60. doi: 10.1016/0165-7992(95)90070-5.
Biochemically active human DNA repair protein, xeroderma pigmentosum G (XPG), was overexpressed in insect cells by a recombinant baculovirus. The recombinant baculovirus produced XPG with a mobility of approximately 185 kDa in a denaturing polyacrylamide gel. Indirect immunofluorescence studies demonstrated that the recombinant full-length XPG protein was expressed predominantly as a nuclear protein. The recombinant XPG protein was purified to apparent homogeneity using Q-sepharose, S-300 size exclusion, and Mono Q column chromatography. XPG protein showed a structure-specific DNA endonuclease activity, and a preferential affinity to single-stranded DNA and RNA compared to double-stranded DNA.
具有生物化学活性的人类DNA修复蛋白——着色性干皮病G蛋白（XPG），通过重组杆状病毒在昆虫细胞中过表达。该重组杆状病毒产生的XPG在变性聚丙烯酰胺凝胶中的迁移率约为185 kDa。间接免疫荧光研究表明，重组全长XPG蛋白主要作为核蛋白表达。使用Q-琼脂糖凝胶、S-300尺寸排阻色谱和Mono Q柱色谱将重组XPG蛋白纯化至表观均一性。XPG蛋白表现出结构特异性DNA内切酶活性，与双链DNA相比，对单链DNA和RNA具有优先亲和力。
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