[Synthesis, cloning, and expression in Escherichia coli cells of human alpha1-antitrypsin cDNA].

cDNA coding for the full-length human alpha 1-antitrypsin (AAT) and its leader sequence has been cloned and sequenced. DNA sequences encoding the deletion variants and a full-length copy of AAT were cloned and expressed under trp-promoter control. It has been shown that guanine replacing right upstream and downstream the ATG of deletion variant increases the expression to ten-fold. The synthesis of deletion AAT in E. coli was evaluated immunologically and the level of the synthesis was shown to be 4-5% of total cellular protein.