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Human placental apurinic/apyrimidinic endonuclease. Its isolation and characterization
- Source :
- Journal of Biological Chemistry. 257:13455-13458
- Publication Year :
- 1982
- Publisher :
- Elsevier BV, 1982.
-
Abstract
- An endonuclease from human placenta has been purified to apparent homogeneity, which acts specifically on DNA containing either apurinic or apyrimidinic sites. The isolation procedure, which results in a 20,000-fold purification and an overall yield of 15%, employs chromatography on a gel of octyl succinic anhydride coupled to agarose by diaminohexane spacers, isoelectric focusing, Sephadex G-75 chromatography, and DNA agarose affinity chromatography. Under conditions in which proteolysis is minimized, this enzyme appears to be the major species of apurinic/apyrimidinic endonuclease. The endonuclease is a monomeric protein with an apparent Mr = 37,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme has a pI of 7.4-7.6, requires Mg2+, is partially stimulated by Mn2+, and is inhibited by EDTA. It has no detectable exonuclease or phosphomonoesterase activity.
Details
- ISSN :
- 00219258
- Volume :
- 257
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi...........c9641fa4641650b7feafbd7b03686948