title: Deoxyribonuclease II from the Icelandic scallop (Chlamys islandica): isolation and partial characterization.
abstract: A deoxyribonuclease (DNase) was isolated from viscera of the cold-adapted marine bivalve Icelandic scallop. The 42 kDa DNase was shown to be a single polypeptide which catalyses DNA hydrolysis in the absence of divalent cations. The isolated enzyme showed maximal activity at pH 6 and no activity above pH 7.2 against native DNA. The scallop DNase was slightly more susceptible to heat denaturation than porcine DNase II and makes double-strand breaks in circular DNA substrate as the porcine enzyme. The N-terminal sequence of the scallop DNase was shown to be closely similar to DNase II (EC 3.1.22.1) proteins from other organisms. The scallop DNase is in addition to plancitoxin I from A. planci, the only DNase II enzyme isolated from marine invertebrates.
authors.affiliation: Marine Biotechnology and Fish Health, Norwegian Institute of Fisheries & Aquaculture, P.O. Box 6122, N-9291 Tromsø, Norway.
authors.forename: Kersti
authors.initials: K
authors.lastname: Øverbø
authors.forename: Bjørnar
authors.initials: B
authors.lastname: Myrnes
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004270:DNA, Circular / Q000737:chemistry*; D004706:Endodeoxyribonucleases / Q000737:chemistry* / Q000302:isolation & purification; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008969:Molecular Sequence Data; D049897:Pectinidae / Q000201:enzymology*; D011489:Protein Denaturation; D013379:Substrate Specificity
chemical_list: D004270:DNA, Circular; D004706:Endodeoxyribonucleases; C019329:deoxyribonuclease II