Biochemistry 1977 Jul 26;1615:3343-7. doi: 10.1021/bi00634a009.

Purification and properties of a 3''-phosphoryl former endodeoxyribonuclease from eggs of Asterias forbesi.

???displayArticle.abstract???
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.

???displayArticle.pubmedLink??? 19046
???displayArticle.link??? Biochemistry