Polynucleotide kinase from a T4 mutant which lacks the 3' phosphatase activity. Journal Article uri icon



  • 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.

publication date

  • March 1, 1978

has restriction

  • green

Date in CU Experts

  • March 13, 2015 12:57 PM

Full Author List

  • Cameron V; Soltis D; Uhlenbeck OC

author count

  • 3

Other Profiles

International Standard Serial Number (ISSN)

  • 0305-1048

Additional Document Info

start page

  • 825

end page

  • 833


  • 5


  • 3