Purification and Properties of the Major Apurinic/Apyrimidinic Endodeoxyribonuclease of Rat‐Liver Chromatin
- 1 September 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 110 (2) , 379-385
- https://doi.org/10.1111/j.1432-1033.1980.tb04878.x
Abstract
Two nucleases active on alkylated-depurinated DNA were extracted from rat liver chromatin with 1 M KCl. The major enzyme was purified to near homogeneity it has a MW of 12,500 (although some dimerization might occur) and needs Mg2+ or Mn2+ for activity. The endonuclease activity is specific for apurinic/apyrimidinic sites in DNA; the enzyme had no associated exonuclease activity.This publication has 31 references indexed in Scilit:
- Cellular Localization of the Apurinic/Apyrimidinic Endodeoxyribonucleases in Rat LiverEuropean Journal of Biochemistry, 1980
- Purification and Characterization of an Endonuclease from Micrococcus luteus that Acts on Depurinated and Carcinogen‐Modified DNAEuropean Journal of Biochemistry, 1978
- A Barley Endonuclease Specific for Apurinic DNAEuropean Journal of Biochemistry, 1978
- Properties of the Main Endonuclease Specific for Apurinic Sites of Escherichia coli (Endonuclease VI)European Journal of Biochemistry, 1978
- A new spectrophotometric assay for protein in cell extractsAnalytical Biochemistry, 1977
- Two enzymes are required for strand incision in repair of alkylated DNANature, 1977
- Purification and characterization of human endonucleases specific for damaged DNABiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1976
- Endonucleases for apurinic sites in plantsFEBS Letters, 1976
- Human endonuclease activity for DNA apurinic sitesNature, 1975
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964