Production of recombinant human glucagon in the form of a fusion protein in Escherichia coli; recovery of glucagon by sequence-specific digestion

Recombinant human glucagon was successfully produced with a high level of expression in Escherichia coli as a fusion protein with human interferon gamma. The synthetic gene was designed to release glucagon, which does not contain glutamic acid residues, from fusion protein with the Staphylococcus au...

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Veröffentlicht in:	Applied microbiology and biotechnology 1992, Vol.36 (4), p.483-486
Hauptverfasser:	ISHIZAKI, J, TAMAKI, M, SHIN, M, TSUZUKI, H, YOSHIKAWA, K, TERAOKA, H, YOSHIDA, N
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acids - analysis Base Sequence Biological and medical sciences Biotechnology Chromatography, High Pressure Liquid Escherichia coli - genetics Fundamental and applied biological sciences. Psychology gamma -interferon Genetic engineering Genetic technics Genome, Human glucagon Glucagon - biosynthesis Glucagon - genetics Glucagon - isolation & purification Humans Interferon-gamma - biosynthesis Interferon-gamma - genetics Methods. Procedures. Technologies Modification of gene expression level Molecular Sequence Data Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - genetics Serine Endopeptidases - metabolism Technology, Pharmaceutical
Online-Zugang:	Volltext
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