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pubmed-article:8829603pubmed:abstractTextActivities 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.lld:pubmed
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pubmed-article:8829603pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:8829603pubmed:articleTitleMulticatalytic proteinase activity in turtle liver: responses to anoxia stress and recovery.lld:pubmed
pubmed-article:8829603pubmed:affiliationInstitute of Biochemistry, Carleton University, Ottawa, Ontario, Canada.lld:pubmed
pubmed-article:8829603pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8829603pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed