JDR Woodhead Publishing
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 Cowman, R. A.
Right arrow Articles by Baron, S. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cowman, R. A.
Right arrow Articles by Baron, S. S.

Journal of Dental Research, Vol 69, 1847-1851, Copyright © 1990 by International & American Associations for Dental Research Online Journals


ARTICLES

Influence of hydrophobicity on oligopeptide utilization by oral streptococci

R. A. Cowman and S. S. Baron
Dental Research Unit, Department of Veterans Affairs Medical Center, Miami, Florida 33125.

The growth responses of Streptococcus mutans VA-29R, Streptococcus sanguis ATCC 10556, and Streptococcus mitior NIH to hydrophilic and hydrophobic peptides obtained following isopropanol fractionation of Trypticase were compared. Although the two fractions contained peptides of similar molecular size, differences were observed with respect to amino acid compositions. S. mutans VA-29R showed a pronounced difference in growth response to hydrophilic vs. hydrophobic peptides. While growth of this micro-organism on hydrophilic peptides was indistinguishable from that on unfractionated Trypticase, only very slow growth occurred on the hydrophobic peptides. S. sanguis ATCC 10556 and S. mitior NIH also displayed some selectivity, as evidenced by their faster relative growth rates on hydrophilic, as compared with hydrophobic, peptides. The results of this study support the conclusion that the properties of the substrate, as defined by its amino acid composition, may be more important than molecular size as a factor influencing recognition and subsequent utilization of oligopeptides as sources of amino acids for growth by these three oral streptococci.


This article has been cited by other articles:


Home page
J. Bacteriol.Home page
H. Tong, W. Chen, W. Shi, F. Qi, and X. Dong
SO-LAAO, a Novel L-Amino Acid Oxidase That Enables Streptococcus oligofermentans To Outcompete Streptococcus mutans by Generating H2O2 from Peptone
J. Bacteriol., July 1, 2008; 190(13): 4716 - 4721.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
J. M. Goldstein, D. Nelson, T. Kordula, J. A. Mayo, and J. Travis
Extracellular Arginine Aminopeptidase from Streptococcus gordonii FSS2
Infect. Immun., February 1, 2002; 70(2): 836 - 843.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. Garault, D. Le Bars, C. Besset, and V. Monnet
Three Oligopeptide-binding Proteins Are Involved in the Oligopeptide Transport of Streptococcus thermophilus
J. Biol. Chem., January 4, 2002; 277(1): 32 - 39.
[Abstract] [Full Text]


Home page
Infect. Immun.Home page
J. M. Goldstein, A. Banbula, T. Kordula, J. A. Mayo, and J. Travis
Novel Extracellular x-Prolyl Dipeptidyl-Peptidase (DPP) from Streptococcus gordonii FSS2: an Emerging Subfamily of Viridans Streptococcal x-Prolyl DPPs
Infect. Immun., September 1, 2001; 69(9): 5494 - 5501.
[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 © 1990 Institutional Access Guidelines