Metalloproteinase of Legionella pneumophila is the major extracellular proteinase of this bacterial species which splits human immunoglobulin G in the hinge region to form the (Fab')2 fragment. This fragment is relatively stable and undergoes further proteolysis at a slow rate. The c' fragment is unstable and is apparently split down to fragments CH2 and CH3.
View Article and Find Full Text PDFAntitryptic activity of human blood serum was decreased after incubation with metalloproteinase from Legionella pneumophila. The enzymatic activity depends on the time of incubation as well as on the ratio between the enzyme content and blood serum total protein. Cross immunoelectrophoresis, involving monospecific rabbit antiserum towards the alpha 1-antitrypsin, demonstrated highly effective hydrolysis of alpha 1-antitrypsin by the metalloproteinase.
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