title: Examination of IgA1-protease activity in Bordetella.
abstract: A total of 43 strains of bacterial genus Bordetella was studied as to the possible extracellular enzyme production responsible for Al-immunoglobulin cleavage. This was observed to be cleaved by 9 of 21 controlled strains of B. pertussis, one of 15 strains of B. parapertussis, and one of 7 strains of B. bronchiseptica. No cleavage of G and M human immunoglobulin classes by protease positive strains of B. pertussis was evaluated. The immunochemical method altogether with polyacrylamide gel electrophoresis (PGE) with sodium dodecyl sulphate (SDS) were used to assess the IgA1 cleavage products bordetella and several compounds belonging to the heavy chain fragments were revealed. The obtained data allowed us to make a presumption that the cleavage sites of peptide chain for bordetella and meningococcal proteases were different ones.
mesh_terms: D001884:Bordetella / Q000201:enzymology*; D007122:Immunoelectrophoresis; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000032:analysis*; D012697:Serine Endopeptidases
chemical_list: D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase