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J. Biochem, 1977, Vol. 81, No. 5 1253-1260
© 1977 Japanese Biochemical Society

research-article

Purification and Properties of Deoxyribonucleic Acid Ligases from Rat Liver1

Hirobumi TERAOKA, Man SHIMOYACHI2 and Kinji TSUKADA

Department of Pathological Biochemistry, Medical Research Institute, Tokyo Medical and Dental University Chiyoda-ku, Tokyo 101

DNA ligases have been purified 1,500-fold from cytoplasmic fraction and 114-fold from 0.15M NaCI 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 is 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.

1This investigation was supported in part by a Grant-in-Aid for Cancer Research from the Ministry of Education, Science and Culture of Japan.

2Present address: Department of Biophysics, Cancer Research Institute, Kanazawa University, Kanazawa, Japan.


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