CHARACTERIZATION OF PROTEASE ACTIVITIES IN CAPNOCYTOPHAGA SPP, PORPHYROMONAS-GINGIVALIS, PREVOTELLA SPP, TREPONEMA-DENTICOLA AND ACTINOBACILLUS-ACTINOMYCETEMCOMITANS
Mi. Gazi et al., CHARACTERIZATION OF PROTEASE ACTIVITIES IN CAPNOCYTOPHAGA SPP, PORPHYROMONAS-GINGIVALIS, PREVOTELLA SPP, TREPONEMA-DENTICOLA AND ACTINOBACILLUS-ACTINOMYCETEMCOMITANS, Oral microbiology and immunology, 12(4), 1997, pp. 240-248
Citations number
43
Categorie Soggetti
Immunology,Microbiology,"Dentistry,Oral Surgery & Medicine
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
.