Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1979-9-17
pubmed:abstractText
The influence of culture media on various properties of Streptococcus mutans was investigated. Strains of S. mutans (serotypes c, d, f, and g) were grown in a complex medium (Todd-Hewitt broth [THB]) or a synthetic medium (SYN). The SYN cells, in contrast to THB cells, did not bind extracellular glucosyltransferase and did not produce in vitro adherence. Both types of cells possessed constitutive levels of glucosyltransferase. B13 cells grown in SYN plus invertase-treated glucose possessed the same level of constitutive enzyme as THB cells. In contrast to THB cells, the SYN cells of seven serotype strains did not agglutinate upon the addition of high-molecular-weight dextran/glucan. Significant quantities of lower-molecular-weight (2 x 10(4) or 7 x 10(4)) dextran and B13 glucan were bound by SYN cells. SYN cells agglutinated weakly in anti-glucan serum (titers, 0 to 16), whereas THB cells possessed titers of 32 to 256. Evidence for the existence of a second binding site in agglutination which does not possess a glucan-like polymer has been obtained. B13 cells grown in invertase-treated THB agglutinated to the same degree as normal THB cells. The nature of this site is unknown. SYN cells possess the type-specific polysaccharide antigen. B13 cells did not bind from THB a glycoprotein which reacts with antisera to the A, B, or T blood group antigens or which allows agglutination upon the addition of dextran. The results demonstrate that S. mutans grown in a chemically defined medium possesse markedly different biochemical and biological activities than cells grown in a complex organic medium.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-1066098, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-1091546, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-1091547, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-1262056, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-1262062, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-1270153, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-13651133, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-14134309, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-14378162, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-361564, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4133332, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4205944, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4205950, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4209387, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4212286, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4353868, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4482, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4515967, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4518082, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4575463, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4582634, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4716541, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4842704, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-4987306, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-5111564, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-5248532, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-5250261, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-5276566, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-5276567, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-5280435, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-5359639, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-55297, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-5784196, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-5791799, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-591060, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-6056776, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-618839, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-669814, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-669817, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-683023, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-825468, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-863516, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-873612, http://linkedlifedata.com/resource/pubmed/commentcorrection/457252-947842
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0019-9567
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
600-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Properties of Streptococcus mutans grown in a synthetic medium: binding of glucosyltransferase and in vitro adherence, and binding of dextran/glucan and glycoprotein and agglutination.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.