JDR JDR Most Read Articles
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Suido, H.
Right arrow Articles by Genco, R. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Suido, H.
Right arrow Articles by Genco, R. J.

Journal of Dental Research, Vol 65, 1335-1340, Copyright © 1986 by International & American Associations for Dental Research Online Journals


ARTICLES

Arylaminopeptidase activities of oral bacteria

H. Suido, M. Nakamura, P. A. Mashimo, J. J. Zambon and R. J. Genco
Department of Oral Biology, School of Dental Medicine, University of New York at Buffalo 14214.

Protease and peptidase enzymes are thought to play a role in the virulence of many oral organisms, especially those associated with periodontal diseases. In order to evaluate the peptidases of periodontopathogens, we compared the arylaminopeptidase activities of Bacteroides gingivalis with those of other oral and non-oral bacteria. Sixty-three bacterial strains representing the prominent cultivable organisms in human periodontal pockets were tested, including representatives of the black-pigmented Bacteroides, Actinobacillus, Actinomyces, Campylobacter, Capnocytophaga, Eikenella, Fusobacterium, Haemophilus, Lactobacillus, Streptococcus, and Veillonella species. Each micro-organism was examined for its ability to hydrolyze 18 synthetic substrates of beta-naphthylamide derivatives of amino acids, dipeptides, and tripeptides. Quantitation of the enzyme activity was accomplished by colorimetric measurement of the amounts of released beta-naphthylamines. N-CBz-glycyl-glycyl-L-arginine-beta-naphthylamide was readily cleaved by B. gingivalis, but slightly or not at all by the other oral strains tested. L-arginine-beta-naphthylamide was cleaved by B. gingivalis, Capnocytophaga species, and Streptococcus species, but not readily by the other Bacteroides strains. Some dipeptide substrates tested, such as glycyl-L-arginine- and glycyl-L-proline-beta-naphthylamide, were strongly cleaved by B. gingivalis and weakly cleaved by other Bacteroides strains. Since high levels of N-CBz-glycyl-glycyl-L-arginyl-aminopeptidase activity are characteristic of B. gingivalis, its measurement may be valuable in the identification of this organism in clinical samples as an aid in diagnosis and monitoring of periodontal infections. Furthermore, this and other aminopeptidases produced by B. gingivalis and other oral organisms may play a role in the tissue destruction seen in periodontal disease.


This article has been cited by other articles:


Home page
Infect. Immun.Home page
Z. E. Juarez and M. W. Stinson
An Extracellular Protease of Streptococcus gordonii Hydrolyzes Type IV Collagen and Collagen Analogues
Infect. Immun., January 1, 1999; 67(1): 271 - 278.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
IADR Journals Advances in Dental Research ®
Journal of Dental Research ® Critical Reviews (1990-2004)
Copyright © 1986 Institutional Access Guidelines