Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
Harmsen, MC; Heeringa, P; van der Geld, YM; Huitema, MG; Klimp, A; Tiran, A; Kallenberg, CG.
Recombinant proteinase 3 (Wegener's antigen) expressed in Pichia pastoris is functionally active and is recognized by patient sera.
Clin Exp Immunol. 1997; 110(2): 257-264.
Doi: 10.1111/j.1365-2249.1997.tb08325.x
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- Co-Autor*innen der Med Uni Graz
- Tiran Andreas
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- Abstract:
- The open reading frame of human proteinase 3 (PR3) without the prepro-peptide was cloned and expressed in Escherichia coli (rcPR3) and in Pichia pastoris (rpPR3). The 6-histidine tagged rpPR3 was efficiently secreted into culture supernatant from which it could be purified by immobilized metal chelate chromatography. Purified rpPR3 migrated as a single 32-kD band on SDS-PAGE and harboured protease activity that could be inhibited with inhibitors specific for serine-proteases. By indirect antigen-capture ELISA using rpPR3, 60% of sera from patients with Wegener's granulomatosis bound to the recombinant product, although it was not recognized in ELISA with directly coated rpPR3.
- Find related publications in this database (using NLM MeSH Indexing)
- Autoantibodies - immunology
- Autoantigens - genetics
- Cloning, Molecular - genetics
- Escherichia coli - genetics
- Humans - genetics
- Myeloblastin - genetics
- Pichia - genetics
- Recombinant Proteins - genetics
- Serine Endopeptidases - genetics
- Wegener Granulomatosis - immunology
- Find related publications in this database (Keywords)
- Wegner's granulomatosis
- recombinant proteinase 3
- human anti-neutrophil cytoplasmic antibody
- Pichia
- expression system