The adsorption of human salivary components to strains of the bacterium Streptococcus mutans.
Using strains of Streptococcus mutans suspended in human saliva, the salivary proteins capable of binding to the surface of the bacteria were identified by immunological and electrophoretic techniques. Six binding components were recognized: IgA, lysozyme, some high molecular weight material (greater than 400,000), probably a glycoprotein, a low molecular weight component (11-13,000), a 150,000 mol. wt protein, and one major component, mol. wt 20-25,000 which did not resolve fully on SDS-polyacrylamide electrophoresis. All these salivary components could be desorbed from the bacteria with 1 M NaCl, and subsequent extraction of the same cells with 6 M guanidine-HCl did not release any more salivary material. The significance of the binding of these salivary components is unknown but some may modify the behaviour of the organisms in vivo.
D000327:Adsorption; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007123:Immunoelectrophoresis, Two-Dimensional; D007070:Immunoglobulin A / Q000032:analysis; D009113:Muramidase / Q000032:analysis; D011485:Protein Binding; D012471:Salivary Proteins and Peptides / Q000032:analysis* / Q000378:metabolism; D013295:Streptococcus mutans / Q000032:analysis* / Q000378:metabolism
D007070:Immunoglobulin A; D012471:Salivary Proteins and Peptides; D009113:Muramidase