期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1970
卷号：65
期号：3
页码：652-659
DOI：10.1073/pnas.65.3.652
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：An enzyme system, purified 560-fold from Escherichia coli infected with bacteriophage T4, catalyzes the formation of a phosphodiester bond between the original 5'-phosphoryl end-group of a DNA strand and a 3'-hydroxyl group of the complementary strand. The product, a terminally cross-linked, spontaneously renaturable DNA duplex, has been characterized by chromatographic analysis, by sedimentation analysis, and by enzymatic digestion. Essential components of the enzyme system, which requires both ATP and Mg++, include the T4-induced DNA ligase and a component found in extracts of uninfected E. coli, which is probably an exonuclease.
