Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1986-3-20
|
pubmed:abstractText |
The objective of this study was to characterize a fraction from oral streptococci containing receptor activity for salivary agglutinin molecules. Several species and strains of streptococci were disrupted in a Ribi press. The supernatant was nuclease-treated and subjected to differential centrifugation. Receptor activity in the fractions was measured by the inhibition of saliva-mediated bacterial aggregation. In addition, bacterial strains were tested for their ability to aggregate and to deplete saliva of agglutinin activity. Three patterns of activity were observed: Streptococcus sanguis M5 depleted saliva of agglutinin activity and aggregated well; Streptococcus sanguis CC5A depleted saliva of agglutinin but did not aggregate well; and Streptococcus faecalis S-161 neither depleted saliva of agglutinin nor did it aggregate. The 105,000 g supernatant fractions derived from Ribi-disrupted Streptococcus sanguis M5 and CC5A, but not from Streptococcus faecalis, showed dose-dependent inhibition of saliva-mediated aggregation. This inhibitory activity was non-dialyzable, had the same heat and trypsin sensitivity as that seen with intact bacteria, and was not due to enzymatic digestion of the salivary agglutinin. Iso-electric focusing revealed a single active region with a pI of 5.5 which was clearly separated from the bulk of the bacterial proteins.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
D
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Agglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Thymidine,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0022-0345
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
65
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
98-104
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
pubmed-meshheading:3080505-Agglutination,
pubmed-meshheading:3080505-Agglutinins,
pubmed-meshheading:3080505-Chromatography, Gel,
pubmed-meshheading:3080505-Chromatography, Ion Exchange,
pubmed-meshheading:3080505-Counterimmunoelectrophoresis,
pubmed-meshheading:3080505-Enterococcus faecalis,
pubmed-meshheading:3080505-Hot Temperature,
pubmed-meshheading:3080505-Humans,
pubmed-meshheading:3080505-Isoelectric Focusing,
pubmed-meshheading:3080505-Receptors, Immunologic,
pubmed-meshheading:3080505-Saliva,
pubmed-meshheading:3080505-Streptococcus sanguis,
pubmed-meshheading:3080505-Thymidine,
pubmed-meshheading:3080505-Tritium,
pubmed-meshheading:3080505-Trypsin
|
pubmed:year |
1986
|
pubmed:articleTitle |
Identification of a Streptococcus sanguis receptor for salivary agglutinins.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|