Purification and properties of a 3'-phosphoryl former endodeoxyribonuclease from eggs of Asterias forbesi.
A DNA endonuclease has been purified from eggs of Asterias forbesi by a simple four-step-purification procedure. The purified enzyme is at least 96% pure and is free of phosphatase, phosphodiesterase, and RNase. It has a pH optimum of 6.5 and does not require divalent cations. The enzyme produces 3'-phosphoryl and 5'-hydroxyl end groups. The products of exhaustive hydrolysis can be grouped in two fractions. The first fraction, 40%, contains a small amount of mononucleotides and di-, tri-, tetra-, penta-, and hexanucleo-tides. The second fraction, 60%, contains oligonucleotides larger than hexanucleotides.
D000818:Animals; D003851:Deoxyribonucleases / Q000302:isolation & purification / Q000378:metabolism; D004447:Echinodermata / Q000201:enzymology*; D004720:Endonucleases / Q000302:isolation & purification / Q000378:metabolism; D005260:Female; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009943:Organophosphorus Compounds / Q000032:analysis; D010063:Ovum / Q000201:enzymology*; D013045:Species Specificity; D013329:Structure-Activity Relationship; D013696:Temperature
D009943:Organophosphorus Compounds; D003851:Deoxyribonucleases; D004720:Endonucleases