High-level Production of Human β-Endorphin in Escherichia coli(Biological Chemistry)

概要

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A human opioid peptide hormone, β-endorphin, was expressed in Escherichia coli as the C-terminal portion of a fused protein. The fused protein consisting of the N-terminal 62% of E. coli anthranilate synthetase (323 amino acids), a peptide corresponding to the linker DNA (7 amino acids), and the precursor form of β-endorphin (47 amino acids), was highly expressed under the control of a tryptophan promoter. The level of expression of β-endorphin was estimated to be 17 mg/liter broth by radioimmunoassay, and 51 mg/liter broth by SDS polyacrylamide gel electrophoresis followed by a densitometric analysis. β-Endorphin was cleaved from the fused protein and purified by HPLC, and is presumed to be indentical with human β-endorphin because of its amino acid composition and amino acid sequence.
社団法人日本農芸化学会の論文
1987-03-22