DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli.
DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation, or ring contraction are functions of endonuclease III in Escherichia coli.
复制标题
因环饱和、断裂或环收缩而受损的胸腺嘧啶残基的 DNA 糖基化酶活性是大肠杆菌中核酸内切酶 III 的功能。
DOI：
--
复制
发表时间：
1984
影响因子：
4.8
通讯作者：
T. Lindahl
中科院分区：
文献类型：
--
作者：
L. Breimer;T. Lindahl
从多聚脱氧核糖核苷酸中切除氧化的、片段化的胸腺嘧啶残基的DNA糖基化酶活性已从大肠杆菌中纯化9，500倍至表观均一性。纯化的酶也能切除胸腺嘧啶乙二醇并在脱嘌呤位点切割DNA，与E.大肠杆菌DNA内切酶III。该酶催化几种不同形式的氧化胸腺嘧啶的释放，包括尿素、甲基酒石酸脲和5-羟基-5-甲基乙内酰脲。天然蛋白质的分子量为25，000，通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳对变性的均质蛋白质获得相同的值。
A DNA glycosylase activity that excises oxidized, fragmented thymine residues from a polydeoxyribonucleotide has been purified 9,500-fold to apparent homogeneity from Escherichia coli. The purified enzyme also excises thymine glycol and cleaves DNA at apurinic sites, and appears to be identical with E. coli DNA endonuclease III. The enzyme catalyzes the release of several different forms of oxidized thymine, including urea, methyltartronylurea and 5-hydroxy-5-methylhydantoin. The molecular weight of the native protein is 25,000, and the same value is obtained for the denatured homogeneous protein by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.