Kieran G. Cloud, Binghui Shen, Gary F. Strniste, Min S. Park
{"title":"XPG protein has a structure-specific endonuclease activity","authors":"Kieran G. Cloud, Binghui Shen, Gary F. Strniste, Min S. Park","doi":"10.1016/0165-7992(95)90070-5","DOIUrl":null,"url":null,"abstract":"<div><p>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 ∼ 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.</p></div>","PeriodicalId":100934,"journal":{"name":"Mutation Research Letters","volume":"347 2","pages":"Pages 55-60"},"PeriodicalIF":0.0000,"publicationDate":"1995-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0165-7992(95)90070-5","citationCount":"37","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Mutation Research Letters","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0165799295900705","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 37
Abstract
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 ∼ 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.
京公网安备 11010802042870号
京ICP备2023020795号-1
分享
求助内容：
应助结果提醒方式：
扫码关注我们
