A method for the amidation of recombinant peptides expressed as intein fusion proteins in Escherichia coli

The increasing use of peptides as pharmaceutical agents, especially in the antiviral and anti-infective therapeutic areas, requires cost-effective production on a large scale 1 . Many peptides need carboxy amidation for full activity or prolonged bioavailability 2 . However, this modification is not...

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Veröffentlicht in:	Nature biotechnology 2001-10, Vol.19 (10), p.974-977
Hauptverfasser:	Cottingham, Ian R., Millar, Alan, Emslie, Elisabeth, Colman, Alan, Schnieke, Angelika E., McKee, Colin
Format:	Artikel
Sprache:	eng
Schlagworte:	Agriculture Amides - metabolism Amino Acid Sequence Amino acids Antibodies Bioavailability Bioinformatics Biological and medical sciences Biomedical and Life Sciences Biomedical Engineering/Biotechnology Biomedicine Biotechnology Cell adhesion & migration Cloning, Molecular - methods E coli Enzymes Escherichia coli Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Genetic Vectors Health. Pharmaceutical industry Heparan sulfate Industrial applications and implications. Economical aspects inteins Life Sciences Milk Molecular Sequence Data Other active biomolecules Peptides Peptides - genetics Peptides - metabolism Production of active biomolecules Protein Processing, Post-Translational Proton-Translocating ATPases - genetics Reagents Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Stem cells technical-report Telomerase Vacuolar Proton-Translocating ATPases
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