Archives of Oral Biology · 1994 · 107 citations · 36 references
AgricultureOral BiologyLactationMilk ChemistryMilk CompositionMilk ProteinsSalivary MicrobiologyAdherenceAnion ExchangeAntimicrobial Activity Of SalivaHuman Milk ProteinsStreptococcal Adhesion In SalivaStreptococci In Milk
Experiments sought to determine the nature of the binding of milk proteins to hydroxyapatite (HA) and to saliva-coated hydroxyapatite (sHA), and to determine the effect of milk and casein on the adherence of Streptococcus mutans GS-5 to sHA. The binding of radiolabelled alpha-casein to HA was reduced when incubated simultaneously with parotid saliva, and enhanced in the presence of milk. The binding of beta- and kappa-casein to HA was unaffected by the presence of parotid saliva and enhanced by the presence of milk. The in vitro bacterial adherence of Strep. mutans GS-5 to sHA beads was reduced when beads were coated with milk instead of buffer, or when bacteria were added to sHA in the presence of milk instead of buffer. Casein proteins (alpha, beta, kappa) added to sHA simultaneously with bacteria inhibited the adherence of Strep. mutans GS-5 to sHA. kappa-Casein, when bound to sHA, inhibited streptococcal adherence to sHA; alpha- and beta-casein, when bound to sHA, had no effect on streptococcal adherence. Fractionation of kappa-casein by anion-exchange chromatography revealed the anti-adherence activity of kappa-casein was mediated primarily by a 40,000 mol. wt. glycoprotein-containing fraction. These data show that milk, particularly kappa-casein fractions, can modulate the adherence of Strep. mutans GS-5 to SHA surfaces in vitro.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
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