High-level production of biologically active human α1-antitrypsin in Escherichia coli

M. Courtney, A. Buchwalder, L. H. Tessier, M. Jaye, A. Benavente, A. Balland, V. Kohli, R. Lathe, P. Tolstoshev, J. P. Lecocq

Research output: Contribution to journalArticlepeer-review


A cDNA clone containing the complete human α1-antitrypsin sequence was isolated from a human liver cDNA bank by screening with a chemically synthesized oligonucleotide probe. DNA sequences encoding the α1-antitrypsin mature polypeptide were inserted into an Escherichia coli expression vector that allows transcription from the efficient leftward promoter of bacteriophage λ (P(L)) and initiation of translation at the λ cII gene ribosome-binding site. This construction resulted in the induction of a 45-kilodalton protein at a level of approximately 15% of total cell protein. The polypeptide produced was recognized by antisera raised against human α1-antitrypsin protein and displayed normal biological activity in an in vitro antielastase assay.

Original languageEnglish
Pages (from-to)669-673
Number of pages5
JournalProceedings of the National Academy of Sciences
Issue number3 I
Publication statusPublished - 1984

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