来自缺乏3'磷酸酶活性的T4突变体的多核苷酸激酶。
Polynucleotide kinase from a T4 mutant which lacks the 3' phosphatase activity.
作者信息
Cameron V, Soltis D, Uhlenbeck O C
出版信息
Nucleic Acids Res. 1978 Mar;5(3):825-33. doi: 10.1093/nar/5.3.825.
Abstract
Polynucleotide kinase from E. coli infected with the PseT 1 mutant of bacteriophage T4 has been isolated. The PseT 1 enzyme purifies similarly to normal polynucleotide kinase and effectively transfers the gamma phosphate of ATP to the 5' terminal hydroxyl of DNA and RNA. The PseT 1 and normal enzymes require similar magnesium ion concentrations, have the same pH optima and are both inhibited by inorganic phosphate. However, the PseT 1 enzyme is totally lacking the 3' phosphatase activity associated with normal polynucleotide kinase. The PseT 1 enzyme is a useful tool for the preparation of oligonucleotides with 3' and 5' terminal phosphates for use as susbstrates for RNA ligase.
摘要
已从感染噬菌体T4的PseT 1突变体的大肠杆菌中分离出多核苷酸激酶。PseT 1酶的纯化方式与正常多核苷酸激酶相似，并能有效地将ATP的γ磷酸基团转移到DNA和RNA的5'末端羟基上。PseT 1酶和正常酶需要相似的镁离子浓度，具有相同的最适pH值，且都受到无机磷酸盐的抑制。然而，PseT 1酶完全缺乏与正常多核苷酸激酶相关的3'磷酸酶活性。PseT 1酶是制备具有3'和5'末端磷酸基团的寡核苷酸的有用工具，这些寡核苷酸可用作RNA连接酶的底物。
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