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.
|Number of pages||5|
|Journal||Proceedings of the National Academy of Sciences|
|Issue number||3 I|
|Publication status||Published - 1984|