Mar 25, 1976

A deoxyribonucleic acid kinase from nuclei of rat liver. Purification and properties

The Journal of Biological Chemistry
C J Levin, S B Zimmerman

Abstract

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.

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Mentioned in this Paper

Cations, Divalent
Phosphate Measurement
Cell Nucleus
Gel Chromatography
Purification Aspects
Nucleotides
Cations, Monovalent
Phosphotransferases
Acids
Polynucleotide 5'-Hydroxyl-Kinase

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