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- W1962804406 abstract "The high-level synthesis of alpha-human atrial natriuretic polypeptide hormone in Escherichia coli has been achieved based on the idea that the yield of a small, basic and unstable polypeptide, such as the natriuretic polypeptide, would be improved by fusion with an appropriate protective polypeptide to construct a neutral fused polypeptide. We prepared an expression vector, pCLaHtrp3t, coding a neutral polypeptide containing 130 amino acid residues in which the polypeptide hormone was fused to a newly designed protective polypeptide through lysine as an enzymatically cleavable residue. The fused polypeptide was synthesized at the high level of 32% of total cellular proteins and at 4.7 X 10(6) molecules per single cell. It was recovered as cellular insoluble fraction and purified to homogeneity. For the isolation of the peptide hormone from the resultant fused polypeptide, Achromobacter protease I, a lysine-specific endopeptidase was used, because it has sufficient activity even in 8 M urea. The recombinant natriuretic polypeptide was indistinguishable from native alpha-human atrial natriuretic polypeptide as regards amino acid sequence as well as biological activity." @default.
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- W1962804406 date "1987-07-01" @default.
- W1962804406 modified "2023-09-26" @default.
- W1962804406 title "Bacterial Synthesis of Recombinant α-Human Atrial Natriuretic Polypeptide" @default.
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- W1962804406 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a122022" @default.
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