Amino-terminal charge affects the periplasmic accumulation of recombinant heregulin/EGF hybrids exported using the Escherichia coli alkaline phosphatase signal sequence

An Escherichia coli expression system that exploits the bacterial alkaline phosphatase (PhoA) signal sequence to translocate recombinant human epidermal growth factor (hEGF) to the periplasm was used to evaluate how changes in the composition and sequence of amino acids near the PhoA-hEGF junction i...

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Veröffentlicht in:	Protein expression and purification 1997-08, Vol.10 (3), p.331
Hauptverfasser:	Campion, S R, Elsasser, E, Chung, R
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkaline Phosphatase - genetics Amino Acid Sequence Base Sequence Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Cell Membrane - metabolism Chromatography, High Pressure Liquid Cytoplasm - metabolism Electrophoresis, Polyacrylamide Gel Epidermal Growth Factor - chemistry Epidermal Growth Factor - genetics Epidermal Growth Factor - isolation & purification Epidermal Growth Factor - metabolism Escherichia coli - genetics Gene Expression Glycoproteins - chemistry Glycoproteins - genetics Glycoproteins - metabolism Humans Molecular Sequence Data Mutagenesis Neuregulin-1 Plasmids - genetics Protein Sorting Signals - chemistry Protein Sorting Signals - genetics Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - isolation & purification Recombinant Fusion Proteins - metabolism Sequence Alignment
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