Home > Publications database > Production and comprehensive quality control of recombinant human interleukin-1 beta: A case study for a process development strategy > print

001     5173
005     20200402205628.0
024 7 _ |2 pmid
|a pmid:18053740
024 7 _ |2 DOI
|a 10.1016/j.pep.2007.09.019
024 7 _ |2 WOS
|a WOS:000252976500017
037 _ _ |a PreJuSER-5173
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemical Research Methods
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
084 _ _ |2 WoS
|a Biotechnology & Applied Microbiology
100 1 _ |a Block, H.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Production and comprehensive quality control of recombinant human interleukin-1 beta: A case study for a process development strategy
260 _ _ |a Orlando, Fla.
|b Academic Press
|c 2008
300 _ _ |a 244 - 254
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Protein Expression and Purification
|x 1046-5928
|0 21001
|y 2
|v 57
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a 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.
536 _ _ |a Programm Biosoft
|c N03
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK443
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Biotechnology: methods
650 _ 2 |2 MeSH
|a Chromatography, Affinity
650 _ 2 |2 MeSH
|a Electrophoresis, Gel, Two-Dimensional
650 _ 2 |2 MeSH
|a Endodeoxyribonucleases: isolation & purification
650 _ 2 |2 MeSH
|a Endoribonucleases: isolation & purification
650 _ 2 |2 MeSH
|a Endotoxins: isolation & purification
650 _ 2 |2 MeSH
|a Exopeptidases: isolation & purification
650 _ 2 |2 MeSH
|a Histidine: metabolism
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Interleukin-1beta: biosynthesis
650 _ 2 |2 MeSH
|a Interleukin-1beta: chemistry
650 _ 2 |2 MeSH
|a Interleukin-1beta: isolation & purification
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Oligopeptides: metabolism
650 _ 2 |2 MeSH
|a Recombinant Proteins: biosynthesis
650 _ 2 |2 MeSH
|a Recombinant Proteins: chemistry
650 _ 2 |2 MeSH
|a Recombinant Proteins: isolation & purification
650 _ 2 |2 MeSH
|a Sequence Analysis, Protein
650 _ 7 |0 0
|2 NLM Chemicals
|a Endotoxins
650 _ 7 |0 0
|2 NLM Chemicals
|a His-His-His-His-His-His
650 _ 7 |0 0
|2 NLM Chemicals
|a Interleukin-1beta
650 _ 7 |0 0
|2 NLM Chemicals
|a Oligopeptides
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Proteins
650 _ 7 |0 71-00-1
|2 NLM Chemicals
|a Histidine
650 _ 7 |0 EC 3.1.-
|2 NLM Chemicals
|a Endodeoxyribonucleases
650 _ 7 |0 EC 3.1.-
|2 NLM Chemicals
|a Endoribonucleases
650 _ 7 |0 EC 3.1.30.2
|2 NLM Chemicals
|a Serratia marcescens nuclease
650 _ 7 |0 EC 3.4.-
|2 NLM Chemicals
|a Exopeptidases
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a Interleukin-1 beta (IL-1 beta)
653 2 0 |2 Author
|a expression screening
653 2 0 |2 Author
|a protein production
653 2 0 |2 Author
|a X-ray crystallography
653 2 0 |2 Author
|a TAGZyme
653 2 0 |2 Author
|a DAPase
653 2 0 |2 Author
|a His-Tag cleavage
653 2 0 |2 Author
|a Immobilized-Metal Affinity Chromatography (IMAC)
653 2 0 |2 Author
|a Ni-NTA
700 1 _ |a Kubicek, J.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Labahn, J.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB886
700 1 _ |a Roth, U.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Schaefer, F.
|b 4
|0 P:(DE-HGF)0
773 _ _ |a 10.1016/j.pep.2007.09.019
|g Vol. 57, p. 244 - 254
|p 244 - 254
|q 57<244 - 254
|0 PERI:(DE-600)1471688-4
|t Protein expression and purification
|v 57
|y 2008
|x 1046-5928
856 7 _ |u http://dx.doi.org/10.1016/j.pep.2007.09.019
909 C O |o oai:juser.fz-juelich.de:5173
|p VDB
913 1 _ |k N03
|v Programm Biosoft
|l BioSoft
|b Schlüsseltechnologien
|z entfällt
|0 G:(DE-Juel1)FUEK443
|x 0
914 1 _ |a übergangsweise lautet die FE-Bezeichnung für das ISB-2 N03
|y 2009
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k ISB-2
|l Molekulare Biophysik
|d 31.12.2010
|g ISB
|0 I:(DE-Juel1)ISB-2-20090406
|x 0
970 _ _ |a VDB:(DE-Juel1)112630
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
980 _ _ |a UNRESTRICTED
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)ISB-2-20090406

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