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  • Title: Expression in Escherichia coli of synthetic human interleukin-1 alpha genes encoding the processed active protein, mutant proteins, and beta-galactosidase fusion proteins.
    Author: Zurawski SM, Pope K, Cherwinski H, Zurawski G.
    Journal: Gene; 1986; 49(1):61-8. PubMed ID: 3106156.
    Abstract:
    We have synthesized, cloned, and expressed the coding region for the C-terminal 159 amino acids (aa) of the human active interleukin polypeptide hormone IL-1 alpha. The sequence was assembled in stages and includes preferred Escherichia coli codons and unique restriction sites. The coding region was cloned on a multicopy plasmid vector adjacent to signals for transcription and translation that directed synthesis of 6% of total E. coli protein as IL-1 alpha. Active IL-1 alpha mutants that have a C-terminal additional eleven aa and that have N-terminal deletions of six and fourteen aa are described. Plasmids expressing beta-galactosidase fusion proteins with various parts of IL-1 alpha at their N-termini were constructed.
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