pubmed-article:8829603 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8829603 | lifeskim:mentions | umls-concept:C0038435 | lld:lifeskim |
pubmed-article:8829603 | lifeskim:mentions | umls-concept:C0041412 | lld:lifeskim |
pubmed-article:8829603 | lifeskim:mentions | umls-concept:C0023884 | lld:lifeskim |
pubmed-article:8829603 | lifeskim:mentions | umls-concept:C2004454 | lld:lifeskim |
pubmed-article:8829603 | lifeskim:mentions | umls-concept:C2247627 | lld:lifeskim |
pubmed-article:8829603 | lifeskim:mentions | umls-concept:C2258865 | lld:lifeskim |
pubmed-article:8829603 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:8829603 | pubmed:dateCreated | 1996-10-17 | lld:pubmed |
pubmed-article:8829603 | 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. | lld:pubmed |
pubmed-article:8829603 | pubmed:language | eng | lld:pubmed |
pubmed-article:8829603 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8829603 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8829603 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8829603 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8829603 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8829603 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8829603 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8829603 | pubmed:month | Mar | lld:pubmed |
pubmed-article:8829603 | pubmed:issn | 1039-9712 | lld:pubmed |
pubmed-article:8829603 | pubmed:author | pubmed-author:StoreyK BKB | lld:pubmed |
pubmed-article:8829603 | pubmed:author | pubmed-author:WillmoreW GWG | lld:pubmed |
pubmed-article:8829603 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8829603 | pubmed:volume | 38 | lld:pubmed |
pubmed-article:8829603 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8829603 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8829603 | pubmed:pagination | 445-51 | lld:pubmed |
pubmed-article:8829603 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:8829603 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8829603 | pubmed:articleTitle | Multicatalytic proteinase activity in turtle liver: responses to anoxia stress and recovery. | lld:pubmed |
pubmed-article:8829603 | pubmed:affiliation | Institute of Biochemistry, Carleton University, Ottawa, Ontario, Canada. | lld:pubmed |
pubmed-article:8829603 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8829603 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |