Studies on nuclear acid deoxyribonucleases and proofreading exonuclease isolated from rat liver nuclei.
Three kinds of deoxyribonucleases (peaks A, B, and C) were separated from purified rat liver nuclei on DEAE-cellulose column chromatography, and their characteristics were partially studied. Peaks A and B had endonuclease activities under acidic conditions with low substrate specificity and did not require divalent metal ions. Peak C had an exonuclease activity under alkaline conditions with substrate specificity for denatured DNA or single stranded homopolymer and required divalent cations. Peak C degraded 3'-terminally mismatched substrate much faster than 3'-terminally matched substrate.
Akiyoshi
H
H
Department of Health Sciences, Faculty of Integrated Arts and Sciences, University of Tokushima.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D002848:Chromatography, DEAE-Cellulose / Q000379:methods; D003851:Deoxyribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D004720:Endonucleases; D005092:Exonucleases / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology / Q000648:ultrastructure*; D008274:Magnesium / Q000494:pharmacology; D008297:Male; D009691:Nucleic Acid Denaturation; D051381:Rats; D013379:Substrate Specificity
D003851:Deoxyribonucleases; D004720:Endonucleases; D005092:Exonucleases; D008274:Magnesium