Deoxyribonuclease II from the Icelandic scallop (Chlamys islandica): isolation and partial characterization

Kersti Øverbø; Bjørnar Myrnes

doi:10.1016/j.cbpb.2005.12.003

Deoxyribonuclease II from the Icelandic scallop (Chlamys islandica): isolation and partial characterization

Comp Biochem Physiol B Biochem Mol Biol. 2006 Mar;143(3):315-8. doi: 10.1016/j.cbpb.2005.12.003. Epub 2006 Jan 19.

Authors

Kersti Øverbø¹, Bjørnar Myrnes

Affiliation

¹ Marine Biotechnology and Fish Health, Norwegian Institute of Fisheries & Aquaculture, P.O. Box 6122, N-9291 Tromsø, Norway.

PMID: 16426884
DOI: 10.1016/j.cbpb.2005.12.003

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Animals
DNA, Circular / chemistry*
Endodeoxyribonucleases / chemistry*
Endodeoxyribonucleases / isolation & purification
Hot Temperature
Hydrogen-Ion Concentration
Hydrolysis
Molecular Sequence Data
Pectinidae / enzymology*
Protein Denaturation
Substrate Specificity

Substances

DNA, Circular
Endodeoxyribonucleases
deoxyribonuclease II