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Localization of the phosphoester bond hydrolyzed by the major apurinic/apyrmidinic endodeoxyribonuclease from rat-liver chromatin.

作者信息

Verly W G, Colson P, Zocchi G, Goffin C, Liuzzi M, Buchsenschmidt G, Muller M

出版信息

Eur J Biochem. 1981 Aug;118(1):195-201. doi: 10.1111/j.1432-1033.1981.tb05505.x.

DOI:10.1111/j.1432-1033.1981.tb05505.x
PMID:6269847
Abstract

The major apurinic/apyrimidinic (AP) endodeoxyribonuclease from rat liver chromatin, an enzyme specific for AP sites in DNA, cleaves the phosphodiester bridge which is the immediate neighbour of the AP site on its 5' side leaving 3'-hydroxyl and 5'-phosphate ends. In contrast with Escherichia coli endonuclease VI, this chromatin enzyme is inactive on reduced AP sites.

摘要

相似文献

1
Localization of the phosphoester bond hydrolyzed by the major apurinic/apyrmidinic endodeoxyribonuclease from rat-liver chromatin.
Eur J Biochem. 1981 Aug;118(1):195-201. doi: 10.1111/j.1432-1033.1981.tb05505.x.
2
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Excision of apurinic sites from DNA with enzymes isolated from rat-liver chromatin.用从大鼠肝脏染色质中分离出的酶切除DNA中的脱嘌呤位点。
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引用本文的文献

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An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro.通用蛋白Kae1的古菌同源物是一种铁金属蛋白，在体外表现出非典型的DNA结合特性和脱嘌呤内切酶活性。
Nucleic Acids Res. 2007;35(18):6042-51. doi: 10.1093/nar/gkm554. Epub 2007 Aug 30.