Purification and characterization of DNase VII, a 3' leads to 5'-directed exonuclease from human placenta.
An exonuclease, DNase VII, has been purified 6000-fold from human placenta. The enzyme has an apparent molecular weight of 43,000, requires Mg2+ for activity, and has a pH optimum of 7.8. The enzyme hydrolyzes single-stranded and nicked duplex DNA at the same rate proceeding in a 3' leads to 5' direction liberating 5'-mononucleotides. It does not measurably hydrolyze polyribonucleotides.
D003851:Deoxyribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D005090:Exodeoxyribonucleases; D005092:Exonucleases / Q000302:isolation & purification / Q000378:metabolism*; D005260:Female; D006801:Humans; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D013379:Substrate Specificity
D003851:Deoxyribonucleases; D005090:Exodeoxyribonucleases; D005092:Exonucleases; C026870:exodeoxyribonuclease VII; D008274:Magnesium