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@ARTICLE{Block:5173,
      author       = {Block, H. and Kubicek, J. and Labahn, J. and Roth, U. and
                      Schaefer, F.},
      title        = {{P}roduction and comprehensive quality control of
                      recombinant human interleukin-1 beta: {A} case study for a
                      process development strategy},
      journal      = {Protein expression and purification},
      volume       = {57},
      issn         = {1046-5928},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PreJuSER-5173},
      pages        = {244 - 254},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {We describe an efficient strategy to produce high-quality
                      proteins by using a single large IMAC chromatography column
                      and enzymatic His-tag removal via the TAGZyme system in
                      pilot scale. Numerous quality assays demonstrated a high
                      purity of the final product, the human cytokine
                      Interleukin-1beta (IL-1beta). The protein preparation was
                      apparently free of host cell proteins, endotoxins, protease,
                      and aggregates. The N-terminal amino acid sequence of
                      IL-1beta was in full agreement with the natural mature form
                      of IL-1beta. The homogeneity of the product was further
                      shown by X-ray structure determination which confirmed the
                      previously solved structure of the protein. We propose the
                      applied workflow as a strategy for industrial production of
                      protein-based biopharmaceuticals.},
      keywords     = {Amino Acid Sequence / Biotechnology: methods /
                      Chromatography, Affinity / Electrophoresis, Gel,
                      Two-Dimensional / Endodeoxyribonucleases: isolation $\&$
                      purification / Endoribonucleases: isolation $\&$
                      purification / Endotoxins: isolation $\&$ purification /
                      Exopeptidases: isolation $\&$ purification / Histidine:
                      metabolism / Humans / Interleukin-1beta: biosynthesis /
                      Interleukin-1beta: chemistry / Interleukin-1beta: isolation
                      $\&$ purification / Models, Molecular / Molecular Sequence
                      Data / Oligopeptides: metabolism / Recombinant Proteins:
                      biosynthesis / Recombinant Proteins: chemistry / Recombinant
                      Proteins: isolation $\&$ purification / Sequence Analysis,
                      Protein / Endotoxins (NLM Chemicals) /
                      His-His-His-His-His-His (NLM Chemicals) / Interleukin-1beta
                      (NLM Chemicals) / Oligopeptides (NLM Chemicals) /
                      Recombinant Proteins (NLM Chemicals) / Histidine (NLM
                      Chemicals) / Endodeoxyribonucleases (NLM Chemicals) /
                      Endoribonucleases (NLM Chemicals) / Serratia marcescens
                      nuclease (NLM Chemicals) / Exopeptidases (NLM Chemicals) / J
                      (WoSType)},
      cin          = {ISB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {Programm Biosoft},
      pid          = {G:(DE-Juel1)FUEK443},
      shelfmark    = {Biochemical Research Methods / Biochemistry $\&$ Molecular
                      Biology / Biotechnology $\&$ Applied Microbiology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18053740},
      UT           = {WOS:000252976500017},
      doi          = {10.1016/j.pep.2007.09.019},
      url          = {https://juser.fz-juelich.de/record/5173},
}