Inactivation of human alpha-1-antitrypsin by a tissue-destructive protease of Legionella pneumophila.
Three extracellular proteases produced by Legionella pneumophila during growth in liquid medium were examined for their effects on human alpha-1-antitrypsin (alpha-1-AT). One of these proteases, tissue-destructive protease (TDP) destroyed completely the trypsin-inhibitory capacity of alpha-1-AT at protease: inhibitor molar ratios down to 0.002:1. After inactivation by TDP, the Mr of alpha-1-AT was reduced by 5000 in SDS-PAGE. This suggested that inactivation entailed only limited cleavage.
D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007875:Legionella / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000494:pharmacology*; D000515:alpha 1-Antitrypsin / Q000097:blood / Q000494:pharmacology*
D000515:alpha 1-Antitrypsin; D010447:Peptide Hydrolases