Linked Life Data

17917700

Source:http://linkedlifedata.com/resource/pubmed/id/17917700

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2008-1-23
pubmed:databankReference
pubmed:abstractText
The Atlantic salmon (Salmo salar) goose-type lysozyme gene was isolated and revealed alternative splicing within exon 2 affecting the signal peptide-encoding region. The lysozyme was produced in Escherichia coli, and the recombinant enzyme showed a high specific lytic activity that was stimulated by low or moderate concentrations of mono- or divalent cations. Relative lytic activities of 70 and 100% were measured at 4 degrees C and 22 degrees C, respectively, and there was no detectable activity at 60 degrees C. However, 30% activity was retained after heating the enzyme for 3 h at 90 degrees C. This unique combination of thermal properties was surprising since the salmon goose-type lysozyme contains no cysteines for protein structure stabilization through disulphide bond formation. The results point to a rapid reversal of inactivation, probably due to instant protein refolding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1420-682X
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2841-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
A cold-active salmon goose-type lysozyme with high heat tolerance.
pubmed:affiliation
Marine Biotechnology and Fish Health, Norwegian Institute of Fisheries & Aquaculture, P.O. Box 6122, N-9291 Tromsø, Norway.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't