Linked Life Data

8829603

Source:http://linkedlifedata.com/resource/pubmed/id/8829603

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-10-17
pubmed:abstractText
Activities of the multicatalytic proteinase complex (MPC) were detected in turtle (Trachemys scripta elegans) liver. The ratio of peptidylglutamyl-peptide bond hydrolyzing, trypsin-like, and chymotrypsin-like activities was 6:2.7:1 for the MPC partially purified by Sepharose CL-6B gel filtration. Molecular mass of the turtle liver enzyme was 940 +/- 46 kD. Nondenaturing PAGE revealed a single band containing MPC activity reacting with peptide substrate. In vivo anoxia exposure (20 h submergence in N2-bubbled water) and subsequent 24 h aerobic recovery stimulated changes in liver protease activity. Peptidylglutamyl-peptide bond hydrolyzing activity of the partially purified MPC increased by 29% during aerobic recovery. Elevated MPC activity during recovery may serve to catabolize specific stress-related proteins or to remove proteins damaged by oxygen free radicals generated upon the reintroduction of oxygen.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
445-51
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Multicatalytic proteinase activity in turtle liver: responses to anoxia stress and recovery.
pubmed:affiliation
Institute of Biochemistry, Carleton University, Ottawa, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't