CHARACTERIZATION OF PROTEASE ACTIVITIES IN CAPNOCYTOPHAGA SPP, PORPHYROMONAS-GINGIVALIS, PREVOTELLA SPP, TREPONEMA-DENTICOLA AND ACTINOBACILLUS-ACTINOMYCETEMCOMITANS

Protease activities in cell sonicates of defined bacterial strains wer e examined using peptide substrates and class-specific inhibitors. Cap nocytophaga SPP, all produced serine dipeptidyl peptidase activity and arginine/lysine, elastase- and chymotrypsin-like enzymes with some me talloprotease characteristics. The elastase-like activity was stronges t in Capnocytophaga sputigena, but the others were greatest in Capnocy tophaga gingivalis. The latter also bad a separate arginine-specific e nzyme which appeared not to be present in the other two species. Porph yromonas gingivalis showed serine dipeptidyl peptidase activity and ve ry strong arginine and lysine cysteine protease activities. Prevotella spp. had inhibitor-resistant dipeptidyl peptidase activity and argini ne cysteine protease activity that was much weaker but biochemically s imilar to P. gingivalis. Treponema denticola possessed a strong trypsi n-like serine protease activity as well as very weak dipeptidyl peptid ase and chymotrypsin-like activities that were sensitive to some cyste ine protease reagents, Actinobacillus actinomycetemcomitans showed a n ovel alanine- and lysine-specific activity, but its nature was unclear .