Document Detail

Human placental apurinic/apyrimidinic endonuclease. Its isolation and characterization.
MedLine Citation:
PMID:  7142159     Owner:  NLM     Status:  MEDLINE    
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.
N L Shaper; R H Grafstrom; L Grossman
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  257     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1982 Nov 
Date Detail:
Created Date:  1983-01-07     Completed Date:  1983-01-07     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  13455-8     Citation Subset:  IM    
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MeSH Terms
DNA-(Apurinic or Apyrimidinic Site) Lyase
Deoxyribonuclease IV (Phage T4-Induced)
Endodeoxyribonucleases / isolation & purification*,  metabolism
Molecular Weight
Placenta / enzymology*
Substrate Specificity
Grant Support
Reg. No./Substance:
EC 3.1.-/Endodeoxyribonucleases; EC IV (Phage T4-Induced); EC or Apyrimidinic Site) Lyase

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