Linked Life Data

6605739

Source:http://linkedlifedata.com/resource/pubmed/id/6605739

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1983-12-17
pubmed:abstractText
The ability of various oral streptococci to bind salivary alpha-amylase to their cell surfaces was investigated. Samples of cells were mixed with whole cleared saliva and the alpha-amylase remaining after removal of the cells was assayed by radial diffusion in starch-containing agarose. Seventy-five per cent of Streptococcus sanguis strains bound the enzyme but strains of Streptococcus mutans and Streptococcus mitior did not. SDS-polyacrylamide gel electrophoretic analysis of Strep. sanguis cells which had been mixed with saliva showed that alpha-amylase is bound to the surface of the cells and can be recovered from them intact. The ability of Strep. sanguis strains to bind the enzyme did not correlate with biotype, IPS production or ability to adhere to saliva-coated hydroxyapatite. The cell-surface receptor responsible for the binding of alpha-amylase to Strep. sanguis (NCTC 7865) is a heat-stable component, possibly protein in nature, which is closely associated with the cell wall.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0003-9969
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
567-73
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
The binding of human salivary alpha-amylase by oral strains of streptococcal bacteria.
pubmed:publicationType
Journal Article