Increased production of low molecular weight recombinant proteins in Escherichia coli
| Autor: | Stephen G. Reams, Stan C. Ly, Rama M. Belagaje, Walter Francis Prouty |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Arginine
Lysine Molecular Sequence Data Gene Expression Biology medicine.disease_cause Biochemistry Cathepsin C chemistry.chemical_compound Residue (chemistry) Methionine medicine Escherichia coli Humans Amino Acid Sequence Cloning Molecular Insulin-Like Growth Factor I Dipeptidyl-Peptidases and Tripeptidyl-Peptidases Molecular Biology Peptide sequence Polyacrylamide gel electrophoresis Proinsulin Base Sequence Peptide Fragments Recombinant Proteins Molecular Weight chemistry Research Article |
| Zdroj: | Protein science : a publication of the Protein Society. 6(9) |
| ISSN: | 0961-8368 |
| Popis: | A general method for obtaining high-level production of low molecular weight proteins in Escherichia coli is described. This method is based on the use of a novel Met-Xaa-protein construction which is formed by insertion of a single amino acid residue (preferably Arginine or Lysine) between the N-terminal methionine and the protein of interest. The utility of this method is illustrated by examples for achieving high-level production of human insulin-like growth factor-1, human proinsulin, and their analogs. Furthermore, highly produced insulin-like growth factor-1 derivatives and human proinsulin analogs are converted to their natural sequences by removal of dipeptides with cathepsin C. |
| Databáze: | OpenAIRE |
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