Skip to main content

Published 2006

Read in Norwegian

Publication details

Journal : Comparative Biochemistry and Physiology - Part B: Biochemistry & Molecular Biology , vol. 143 , p. 315–318 , 2006

Publisher : Elsevier

International Standard Numbers :
Printed : 1096-4959
Electronic : 1879-1107

Publication type : Academic article

Contributors : Øverbø, Kersti; Myrnes, Bjørnar

If you have questions about the publication, you may contact Nofima’s Chief Librarian.

Kjetil Aune
Chief Librarian


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 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.
© 2005 Elsevier Inc. All rights reserved.