Characterization of Legumain

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dc.contributor.authorSchwarz, Gerold
dc.contributor.authorBrandenburg, Jens
dc.contributor.authorReich, Michael
dc.contributor.authorBurster, Timo
dc.contributor.authorDriessen, Christoph
dc.contributor.authorKalbacher, Hubert
dc.date.accessioned2018-08-20T09:06:42Z
dc.date.available2018-08-20T09:06:42Z
dc.date.issued2002-11
dc.description.abstractThe mammalian legumain, also called asparaginyl endopeptidase (AEP), is critically involved in the processing of bacterial antigens for MHC class II presentation. In order to investigate the substrate specificity of AEP in the P1’ position, we created a peptide library and digested it with purified pig kidney AEP. Digestion was less efficient only when proline was in the P1’ position. Maximum AEP activity was found in lysosomal fractions of different types of antigen presenting cells (APC). When the multiple sclerosis-associated autoantigen myelin basic protein (MBP) was digested with AEP, the immunodominant epitope 83 – 99 was destroyed. Myoglobin as an alternative substrate was AEP resistant. These results suggest an important, but not necessarily critical role for AEP in lysosomal antigen degradationen_US
dc.identifier.citationGerold Schwarz, Jens Brandenburg, Michael Reich, Timo Burster, Christoph Driessen and Hubert Kalbacher. 2002. Characterization of Legumain. Biological Chemistry. Vol. 383. pp. 1813 – 1816.en_US
dc.identifier.urihttp://nur.nu.edu.kz/handle/123456789/3388
dc.language.isoenen_US
dc.publisherBiological Chemistryen_US
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.subjectAntigen processingen_US
dc.subjectCysteine endopeptidaseen_US
dc.subjectSubstrate specificityen_US
dc.titleCharacterization of Legumainen_US
dc.typeArticleen_US
workflow.import.sourcescience

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