A deoxyribonucleic acid kinase from nuclei of rat liver. Purification and properties.
A DNA kinase has been partially purified from rat liver nuclei by a procedure which also yields DNA ligase. The kinase uses ATP to phosphorylate specifically the 5'-hydroxyl termini of oligodeoxynucleotides and of single- or double-stranded DNA, yielding 5'-phosphate termini and ADP. The kinase is inactive on RNA, or on oligodeoxynucleotides of chain length less than approximately 10 to 12 residues. The kinase requires a divalent cation (Mg2+, Mn2+, Co2+, Zn2+, Ni2+, or Ca2+) for activity and has an acidic pH optimum. It is inhibited by a variety of nucleotides as well as by very low levels of inorganic and organic sulfate compounds and sulfate analogues. The molecular weight of the kinase is estimated to be 8 times 10(4) from gel filtration.
D000818:Animals; D002413:Cations, Divalent; D002414:Cations, Monovalent; D002467:Cell Nucleus / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009994:Osmolar Concentration; D010770:Phosphotransferases / Q000378:metabolism*; D011116:Polynucleotide 5'-Hydroxyl-Kinase / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats
D002413:Cations, Divalent; D002414:Cations, Monovalent; D010770:Phosphotransferases; D011116:Polynucleotide 5'-Hydroxyl-Kinase