@article{Gotze2013-04-15Pitfa-50116,
  year={2013},
  doi={10.1242/jeb.082792},
  title={Pitfalls in invertebrate proteasome assays},
  number={8},
  volume={216},
  issn={0022-0949},
  journal={The Journal of Experimental Biology},
  pages={1351--1354},
  author={Götze, Sandra and Bose, Aneesh P. H. and Abele, Doris and Sokolova, Inna M. and Saborowski, Reinhard}
}

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    <dc:contributor>Abele, Doris</dc:contributor>
    <dc:creator>Götze, Sandra</dc:creator>
    <dc:creator>Saborowski, Reinhard</dc:creator>
    <dc:contributor>Saborowski, Reinhard</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2020-07-03T11:59:19Z</dc:date>
    <dc:contributor>Bose, Aneesh P. H.</dc:contributor>
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    <dc:contributor>Götze, Sandra</dc:contributor>
    <dc:creator>Sokolova, Inna M.</dc:creator>
    <dc:contributor>Sokolova, Inna M.</dc:contributor>
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    <dcterms:abstract xml:lang="eng">The ubiquitin-proteasome system controls a variety of essential intracellular processes through directed protein turnover. The invertebrate proteasome has recently gained increasing interest with respect to central physiological processes and pathways in different taxa. A pitfall in proteasome activity assays, represented by the trypsin-like, chymotrypsin-like or caspase-like site, lies in the fact that most commonly used experimental substrates are susceptible to degradation by non-proteasomal proteolytic enzymes, which can lead to erroneous interpretation of activity data obtained. Through the use of a proteasome-specific inhibitor, epoxomicin, we showed that the shares of proteasomal and non-proteasomal activities in the degradation of a model polypeptide substrate for chymotrypsin-like activity vary considerably between invertebrate taxa. Crustacean muscle tissue and hemocytes showed almost exclusively proteasomal activity. In yeast, approximately 90% of total proteolytic activity can be attributed to the proteasome. In contrast, proteasomal activity comprises only 20-60% of the total proteolytic activity in bivalve tissues. These results reveal that, without verification of the shares of proteasomal and non-proteasomal activities in crude extracts through the use of highly specific inhibitors, common proteasomal enzyme assays should be used and interpreted with caution.</dcterms:abstract>
    <dcterms:issued>2013-04-15</dcterms:issued>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/50116"/>
    <dcterms:title>Pitfalls in invertebrate proteasome assays</dcterms:title>
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    <dc:creator>Abele, Doris</dc:creator>
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