Purification and properties of deoxyribonucleic acid ligases from rat liver.
DNA ligases have been purified 1,500-fold cytoplasmic fraction and 114-fold from 0.15 M NaCl extract of rat-liver nuclei. These enzymes catalyze the formation of a phosphodiester linkage between the 3'-hydroxyl group and the 5'-phosphoryl group of an interrupted strand in a DNA duplex. The enzyme from each fraction requires ATP and Mg2+ (or Mn2+) for activity, and its inhibited reversibly by p-chloromercuribenzoate. The cytoplasmic and nuclear enzymes are distinguished from each other by the following criteria: apparent molecular weight; sedimentation coefficient; charge properties; Km for Mg2+ (or Mn2+); Km for ATP; effect of ionic strength on the molecular and kinetic properties.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D004789:Enzyme Activation; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D008297:Male; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D011118:Polynucleotide Ligases / Q000302:isolation & purification / Q000378:metabolism; D011189:Potassium Chloride / Q000494:pharmacology; D051381:Rats
D008345:Manganese; D011189:Potassium Chloride; D000255:Adenosine Triphosphate; D011118:Polynucleotide Ligases; D008274:Magnesium