Document Detail


pH change in artificial dental plaque formed by glucosyltransferase and some oral bacteria during batch and continuous culture.
MedLine Citation:
PMID:  3156164     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Streptococcus mutans alone or cell-free glucosyltransferase (G-Tase)-together with either Streptococcus sanguis, Streptococcus salivarius, Actinomyces viscosus, or Lactobacillus casei cells-formed artificial dental plaque that firmly adhered to glass electrodes in a continuous culture system containing sucrose. The pH in these artificial plaque samples decreased more than did that of the surrounding medium. In the absence of GTase, the bacteria other than S. mutans did not form firmly-adhering plaque on glass electrodes. The pH of the plaque formed with GTase alone did not show the pH decrease seen when the plaque contained bacteria, but, because it catalyzed the synthesis of glucan, it is suggested that the glucan acts as a diffusion barrier to retard acid loss from plaque containing acid-producing bacteria.
Authors:
T Takehara; M Itoh; N Hanada; E Saeki
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of dental research     Volume:  64     ISSN:  0022-0345     ISO Abbreviation:  J. Dent. Res.     Publication Date:  1985 Mar 
Date Detail:
Created Date:  1985-04-19     Completed Date:  1985-04-19     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  0354343     Medline TA:  J Dent Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  447-9     Citation Subset:  D; IM    
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MeSH Terms
Descriptor/Qualifier:
Actinomyces / physiology*
Adhesiveness
Bacteriological Techniques
Dental Plaque / microbiology,  physiopathology*
Glucans / metabolism
Glucosyltransferases / pharmacology*
Humans
Hydrogen-Ion Concentration
Lactobacillus / physiology*
Streptococcus / physiology*
Streptococcus mutans / enzymology,  physiology
Streptococcus sanguis / metabolism,  physiology
Chemical
Reg. No./Substance:
0/Glucans; EC 2.4.1.-/Glucosyltransferases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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